S00057
type: Enzyme
active site residues resources: P22303
active site residues resources: P04058
active site residues resources: 1acj
cath: Rossmann fold
csa: 2ace
ec: https://purl.uniprot.org/enzyme/3.1.1.7
kegg enzyme: acetylcholinesterase
kegg intermediate: Peptidyl-Ser-tetrahedral intermediate (with previous acetylcholine carboxylic-ester)
kegg intermediate: Acetyl-enzyme (Peptidyl-Ser-acetyl group)
kegg intermediate: Peptidyl-Ser-acetyl-tetrahedral-intermediate
kegg pathway: Glycerophospholipid metabolism
kegg product: Choline
kegg product: Acetate
kegg substrate: Acetylcholine
kegg substrate: H2O
pdb: 1acjA
pdb: 1aclA
pdb: 1amnA
pdb: 1ax9A
pdb: 1cfjA
pdb: 1dx6A
pdb: 1e3qA
pdb: 1e66A
pdb: 1ea5A
pdb: 1eeaA
pdb: 1eveA
pdb: 1fssA
pdb: 1gpkA
pdb: 1gpnA
pdb: 1gqrA
pdb: 1gqsA
pdb: 1h22A
pdb: 1h23A
pdb: 1hbjA
pdb: 1jjbA
pdb: 1oceA
pdb: 1qidA
pdb: 1qieA
pdb: 1qifA
pdb: 1qigA
pdb: 1qihA
pdb: 1qiiA
pdb: 1qijA
pdb: 1qikA
pdb: 1qimA
pdb: 1qtiA
pdb: 1somA
pdb: 1votA
pdb: 1vxoA
pdb: 1vxrA
pdb: 1w4lA
pdb: 1w6rA
pdb: 1w75A
pdb: 1w75B
pdb: 1w76A
pdb: 1w76B
pdb: 2aceA
pdb: 2ackA
pdb: 2dfpA
pdb: 1b41A
pdb: 1f8uA
rlcp: p14
uniprot: P04058
uniprot: P22303
references: Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein.
references: Substrate inhibition of acetylcholinesterase: residues affecting signal transduction from the surface to the catalytic center.
references: 1.9-A resolution structure of fasciculin 1, an anti-acetylcholinesterase toxin from green mamba snake venom.
references: Mutagenesis of human acetylcholinesterase. Identification of residues involved in catalytic activity and in polypeptide folding.
references: Excavations into the active-site gorge of cholinesterases.
references: Three-dimensional structure of acetylcholinesterase and of its complexes with anticholinesterase drugs.
references: Engineering resistance to 'aging' of phosphylated human acetylcholinesterase. Role of hydrogen bond network in the active center.
references: Key active site residues in the inhibition of acetylcholinesterases by soman.
references: Quaternary ligand binding to aromatic residues in the active-site gorge of acetylcholinesterase.
references: Three-dimensional structures of acetylcholinesterase and of its complexes with anticholinesterase agents.
references: Molecular recognition in acetylcholinesterase catalysis: free-energy correlations for substrate turnover and inhibition by trifluoro ketone transition-state analogs.
references: Structure and dynamics of the active site gorge of acetylcholinesterase: synergistic use of molecular dynamics simulation and X-ray crystallography.
references: Open "back door" in a molecular dynamics simulation of acetylcholinesterase.
references: Allosteric modulation of acetylcholinesterase activity by peripheral ligands involves a conformational transition of the anionic subsite.
references: Acetylcholinesterase inhibition by fasciculin: crystal structure of the complex.

Rossmann fold
type: Cath
catalytic domain: index.html
references: http://www.cathdb.info/version/latest/superfamily/3.40.50.1820

H2O
type: KeggSubstrate
compound type: H2O
references: KEGG:C00001
references: CHEBI:15377
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Glycerophospholipid metabolism
type: KeggPathway
references: KEGG:MAP00564

Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein.
type: BibliographicResource
authors:
  item: Sussman JL
  item: Harel M
  item: Frolow F
  item: Oefner C
  item: Goldman A
  item: Toker L
  item: Silman I
journal: Science
medline id: 91343928
pages: 872-9
published year: 1991
volume: 253
references: http://www.ncbi.nlm.nih.gov/pubmed/1678899
references: P04058
comment: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

Three-dimensional structures of acetylcholinesterase and of its complexes with anticholinesterase agents.
type: BibliographicResource
authors:
  item: Silman I
  item: Harel M
  item: Axelsen P
  item: Raves M
  item: Sussman JL
journal: Biochem Soc Trans
pages: 745-9
published year: 1994
volume: 22
references: http://www.ncbi.nlm.nih.gov/pubmed/7821677

Molecular recognition in acetylcholinesterase catalysis: free-energy correlations for substrate turnover and inhibition by trifluoro ketone transition-state analogs.
type: BibliographicResource
authors:
  item: Nair HK
  item: Seravalli J
  item: Arbuckle T
  item: Quinn DM
journal: Biochemistry
pages: 8566-76
published year: 1994
volume: 33
references: http://www.ncbi.nlm.nih.gov/pubmed/8031791

Structure and dynamics of the active site gorge of acetylcholinesterase: synergistic use of molecular dynamics simulation and X-ray crystallography.
type: BibliographicResource
authors:
  item: Axelsen PH
  item: Harel M
  item: Silman I
  item: Sussman JL
journal: Protein Sci
pages: 188-97
published year: 1994
volume: 3
references: http://www.ncbi.nlm.nih.gov/pubmed/8003956

Open "back door" in a molecular dynamics simulation of acetylcholinesterase.
type: BibliographicResource
authors:
  item: Gilson MK
  item: Straatsma TP
  item: McCammon JA
  item: Ripoll DR
  item: Faerman CH
  item: Axelsen PH
  item: Silman I
  item: Sussman JL
journal: Science
pages: 1276-8
published year: 1994
volume: 263
references: http://www.ncbi.nlm.nih.gov/pubmed/8122110

Allosteric modulation of acetylcholinesterase activity by peripheral ligands involves a conformational transition of the anionic subsite.
type: BibliographicResource
authors:
  item: Barak D
  item: Ordentlich A
  item: Bromberg A
  item: Kronman C
  item: Marcus D
  item: Lazar A
  item: Ariel N
  item: Velan B
  item: Shafferman A
journal: Biochemistry
pages: 15444-52
published year: 1995
volume: 34
references: http://www.ncbi.nlm.nih.gov/pubmed/7492545

Acetylcholinesterase inhibition by fasciculin: crystal structure of the complex.
type: BibliographicResource
authors:
  item: Bourne Y
  item: Taylor P
  item: Marchot P
journal: Cell
pages: 503-12
published year: 1995
volume: 83
references: http://www.ncbi.nlm.nih.gov/pubmed/8521480

Contribution of aromatic moieties of tyrosine 133 and of the anionic subsite tryptophan 86 to catalytic efficiency and allosteric modulation of acetylcholinesterase.
type: BibliographicResource
authors:
  item: Ordentlich A
  item: Barak D
  item: Kronman C
  item: Ariel N
  item: Segall Y
  item: Velan B
  item: Shafferman A
journal: J Biol Chem
pages: 2082-91
published year: 1995
volume: 270
references: http://www.ncbi.nlm.nih.gov/pubmed/7836436

Allosteric control of acetylcholinesterase catalysis by fasciculin.
type: BibliographicResource
authors:
  item: Radic Z
  item: Quinn DM
  item: Vellom DC
  item: Camp S
  item: Taylor P
journal: J Biol Chem
pages: 20391-9
published year: 1995
volume: 270
references: http://www.ncbi.nlm.nih.gov/pubmed/7657613

Theoretical analysis of the structure of the peptide fasciculin and its docking to acetylcholinesterase.
type: BibliographicResource
authors:
  item: van den Born HK
  item: Radic Z
  item: Marchot P
  item: Taylor P
  item: Tsigelny I
journal: Protein Sci
pages: 703-15
published year: 1995
volume: 4
references: http://www.ncbi.nlm.nih.gov/pubmed/7613468

Crystal structure of an acetylcholinesterase-fasciculin complex: interaction of a three-fingered toxin from snake venom with its target.
type: BibliographicResource
authors:
  item: Harel M
  item: Kleywegt GJ
  item: Ravelli RB
  item: Silman I
  item: Sussman JL
journal: Structure
medline id: 96363673
pages: 1355-66
published year: 1995
volume: 3
references: http://www.ncbi.nlm.nih.gov/pubmed/8747462
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P04058
comment: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF COMPLEX WITH FASCICULIN.

Substrate inhibition of acetylcholinesterase: residues affecting signal transduction from the surface to the catalytic center.
type: BibliographicResource
authors:
  item: Shafferman A
  item: Ariel N
  item: Velan B
  item: Ordentlich A
  item: Kronman C
  item: Grosfeld H
  item: Leitner M
  item: Flashner Y
  item: Cohen S
  item: Barak D
journal: EMBO J
pages: 3561-8
published year: 1992
volume: 11
references: http://www.ncbi.nlm.nih.gov/pubmed/1396557

Aging of phosphylated human acetylcholinesterase: catalytic processes mediated by aromatic and polar residues of the active centre.
type: BibliographicResource
authors:
  item: Shafferman A
  item: Ordentlich A
  item: Barak D
  item: Stein D
  item: Ariel N
  item: Velan B
journal: Biochem J
pages: 833-40
published year: 1996
volume: 318
references: http://www.ncbi.nlm.nih.gov/pubmed/8836126

Aspartate 74 as a primary determinant in acetylcholinesterase governing specificity to cationic organophosphonates.
type: BibliographicResource
authors:
  item: Hosea NA
  item: Radic Z
  item: Tsigelny I
  item: Berman HA
  item: Quinn DM
  item: Taylor P
journal: Biochemistry
pages: 10995-1004
published year: 1996
volume: 35
references: http://www.ncbi.nlm.nih.gov/pubmed/8718893

Site-directed mutants designed to test back-door hypotheses of acetylcholinesterase function.
type: BibliographicResource
authors:
  item: Faerman C
  item: Ripoll D
  item: Bon S
  item: Le Feuvre Y
  item: Morel N
  item: Massoulie J
  item: Sussman JL
  item: Silman I
journal: FEBS Lett
pages: 65-71
published year: 1996
volume: 386
references: http://www.ncbi.nlm.nih.gov/pubmed/8635606

Structural modifications of the omega loop in human acetylcholinesterase.
type: BibliographicResource
authors:
  item: Velan B
  item: Barak D
  item: Ariel N
  item: Leitner M
  item: Bino T
  item: Ordentlich A
  item: Shafferman A
journal: FEBS Lett
pages: 22-8
published year: 1996
volume: 395
references: http://www.ncbi.nlm.nih.gov/pubmed/8849682

The X-ray structure of a transition state analog complex reveals the molecular origins of the catalytic power and substrate specificity of acetylcholinesterase.
type: BibliographicResource
authors:
  item: Harel M
  item: Quinn DM
  item: Nair HK
  item: Silman I
  item: Sussman JL
journal: J Am Chem Soc
pages: 2340-6
published year: 1996
volume: 118
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Soluble monomeric acetylcholinesterase from mouse: expression, purification, and crystallization in complex with fasciculin.
type: BibliographicResource
authors:
  item: Marchot P
  item: Ravelli RB
  item: Raves ML
  item: Bourne Y
  item: Vellom DC
  item: Kanter J
  item: Camp S
  item: Sussman JL
  item: Taylor P
journal: Protein Sci
pages: 672-9
published year: 1996
volume: 5
references: http://www.ncbi.nlm.nih.gov/pubmed/8845756

Studies on a new series of THA analogues: effects of the aromatic residues that line the gorge of AChE.
type: BibliographicResource
authors:
  item: Pomponi M
  item: Marta M
  item: Colella A
  item: Sacchi S
  item: Patamia M
  item: Gatta F
  item: Capone F
  item: Oliverio A
  item: Pavone F
journal: FEBS Lett
pages: 155-60
published year: 1997
volume: 409
references: http://www.ncbi.nlm.nih.gov/pubmed/9202137

Structure of acetylcholinesterase complexed with the nootropic alkaloid, (-)-huperzine A.
type: BibliographicResource
authors:
  item: Raves ML
  item: Harel M
  item: Pang YP
  item: Silman I
  item: Kozikowski AP
  item: Sussman JL
journal: Nat Struct Biol
medline id: 97143314
pages: 57-63
published year: 1997
volume: 4
references: http://www.ncbi.nlm.nih.gov/pubmed/8989325
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P04058
comment: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

Molecular mechanic study of nerve agent O-ethyl S-[2-(diisopropylamino)ethyl]methylphosphonothioate (VX) bound to the active site of Torpedo californica acetylcholinesterase.
type: BibliographicResource
authors:
  item: Albaret C
  item: Lacoutiere S
  item: Ashman WP
  item: Froment D
  item: Fortier PL
journal: Proteins
pages: 543-55
published year: 1997
volume: 28
references: http://www.ncbi.nlm.nih.gov/pubmed/9261870

Static Laue diffraction studies on acetylcholinesterase.
type: BibliographicResource
authors:
  item: Ravelli RB
  item: Raves ML
  item: Ren Z
  item: Bourgeois D
  item: Roth M
  item: Kroon J
  item: Silman I
  item: Sussman JL
journal: Acta Crystallogr D Biol Crystallogr
pages: 1359-66
published year: 1998
volume: 54
references: http://www.ncbi.nlm.nih.gov/pubmed/10089512
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

1.9-A resolution structure of fasciculin 1, an anti-acetylcholinesterase toxin from green mamba snake venom.
type: BibliographicResource
authors:
  item: le Du MH
  item: Marchot P
  item: Bougis PE
  item: Fontecilla-Camps JC
journal: J Biol Chem
pages: 22122-30
published year: 1992
volume: 267
references: http://www.ncbi.nlm.nih.gov/pubmed/1429564

The 'aromatic patch' of three proximal residues in the human acetylcholinesterase active centre allows for versatile interaction modes with inhibitors.
type: BibliographicResource
authors:
  item: Ariel N
  item: Ordentlich A
  item: Barak D
  item: Bino T
  item: Velan B
  item: Shafferman A
journal: Biochem J
pages: 95-102
published year: 1998
volume: 335
references: http://www.ncbi.nlm.nih.gov/pubmed/9742217

The role of TRP84 in catalytic power and the specificity of AChE.
type: BibliographicResource
authors:
  item: Pomponi M
  item: Sacchi S
  item: Colella A
  item: Patamia M
  item: Marta M
journal: Biophys Chem
pages: 239-46
published year: 1998
volume: 72
references: http://www.ncbi.nlm.nih.gov/pubmed/9691268

Three-dimensional structure of a complex of E2020 with acetylcholinesterase from Torpedo californica.
type: BibliographicResource
authors:
  item: Kryger G
  item: Silman I
  item: Sussman JL
journal: J Physiol Paris
pages: 191-4
published year: 1998
volume: 92
references: http://www.ncbi.nlm.nih.gov/pubmed/9789806

Quaternary structure of tetrameric acetylcholinesterase.
type: BibliographicResource
authors:
  item: Raves ML
  item: Giles K
  item: Schrag JD
  item: Schmid MF
  item: Phillips GN
  item: Wah C
  item: Howard AJ
  item: Silman I
  item: Sussman JL
journal: Structure and Function of Cholinesterases and Related Proteins
published year: 1998
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography (ISBN: 0306460505)

"Back door" opening implied by the crystal structure of a carbamoylated acetylcholinesterase.
type: BibliographicResource
authors:
  item: Bartolucci C
  item: Perola E
  item: Cellai L
  item: Brufani M
  item: Lamba D
journal: Biochemistry
medline id: 99249780
pages: 5714-9
published year: 1999
volume: 38
references: http://www.ncbi.nlm.nih.gov/pubmed/10231521
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P04058
comment: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).

Phosphoryl oxime inhibition of acetylcholinesterase during oxime reactivation is prevented by edrophonium.
type: BibliographicResource
authors:
  item: Luo C
  item: Saxena A
  item: Smith M
  item: Garcia G
  item: Radic Z
  item: Taylor P
  item: Doctor BP
journal: Biochemistry
pages: 9937-47
published year: 1999
volume: 38
references: http://www.ncbi.nlm.nih.gov/pubmed/10433700

Crystal structures of aged phosphonylated acetylcholinesterase: nerve agent reaction products at the atomic level.
type: BibliographicResource
authors:
  item: Millard CB
  item: Silman I
  item: Sussman JL
  item: Kryger G
  item: Ordentlich A
  item: Greenblatt HM
  item: Harel M
  item: Raves ML
  item: Segall Y
  item: Barak D
  item: Shafferman A
journal: Biochemistry
medline id: 99282167
pages: 7032-9
published year: 1999
volume: 38
references: http://www.ncbi.nlm.nih.gov/pubmed/10353814
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P04058
comment: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

Structure of acetylcholinesterase complexed with (-)-galanthamine at 2.3 A resolution.
type: BibliographicResource
authors:
  item: Greenblatt HM
  item: Kryger G
  item: Lewis T
  item: Silman I
  item: Sussman JL
journal: FEBS Lett
medline id: 20074924
pages: 321-6
published year: 1999
volume: 463
references: http://www.ncbi.nlm.nih.gov/pubmed/10606746
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P04058
comment: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

Reaction products of acetylcholinesterase and VX reveal a mobile histidine in the catalytic triad.
type: BibliographicResource
authors:
  item: Millard CB
  item: Koellner G
  item: Ordentlich A
  item: Shafferman A
  item: Silman I
  item: Sussman JL
journal: J Am Chem Soc
pages: 9883-4
published year: 1999
volume: 121
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Conformational flexibility of the acetylcholinesterase tetramer suggested by x-ray crystallography.
type: BibliographicResource
authors:
  item: Bourne Y
  item: Grassi J
  item: Bougis PE
  item: Marchot P
journal: J Biol Chem
pages: 30370-6
published year: 1999
volume: 274
references: http://www.ncbi.nlm.nih.gov/pubmed/10521413
references: P04058

Mutagenesis of human acetylcholinesterase. Identification of residues involved in catalytic activity and in polypeptide folding.
type: BibliographicResource
authors:
  item: Shafferman A
  item: Barak D
  item: et al
  item: Kronman C
  item: Flashner Y
  item: Leitner M
  item: Grosfeld H
  item: Ordentlich A
  item: Gozes Y
  item: Cohen S
  item: Ariel N
journal: J Biol Chem
medline id: 92388112
pages: 17640-8
published year: 1992
volume: 267
references: http://www.ncbi.nlm.nih.gov/pubmed/1517212
references: P22303
comment: MUTAGENESIS OF ACTIVE SITE RESIDUES AND OF ASP-206 AND ASP-435.

Crystal structure of mouse acetylcholinesterase. A peripheral site-occluding loop in a tetrameric assembly.
type: BibliographicResource
authors:
  item: Bourne Y
  item: Taylor P
  item: Bougis PE
  item: Marchot P
journal: J Biol Chem
pages: 2963-70
published year: 1999
volume: 274
references: http://www.ncbi.nlm.nih.gov/pubmed/9915834

Predicting relative binding free energies of tacrine-huperzine A hybrids as inhibitors of acetylcholinesterase.
type: BibliographicResource
authors:
  item: Barril X
  item: Orozco M
  item: Luque FJ
journal: J Med Chem
pages: 5110-9
published year: 1999
volume: 42
references: http://www.ncbi.nlm.nih.gov/pubmed/10602696

Structure of acetylcholinesterase complexed with E2020 (Aricept): implications for the design of new anti-Alzheimer drugs.
type: BibliographicResource
authors:
  item: Kryger G
  item: Silman I
  item: Sussman JL
journal: Structure Fold Des
medline id: 99197295
pages: 297-307
published year: 1999
volume: 7
references: http://www.ncbi.nlm.nih.gov/pubmed/10368299
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P04058
comment: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

Structures of recombinant native and E202Q mutant human acetylcholinesterase complexed with the snake-venom toxin fasciculin-II.
type: BibliographicResource
authors:
  item: Kryger G
  item: Shafferman A
  item: Silman I
  item: Sussman JL
  item: Harel M
  item: Giles K
  item: Toker L
  item: Velan B
  item: Lazar A
  item: Kronman C
  item: Barak D
  item: Ariel N
journal: Acta Crystallogr D Biol Crystallogr
medline id: 20508217
pages: 1385-94
published year: 2000
volume: 56
references: http://www.ncbi.nlm.nih.gov/pubmed/11053835
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P22303
comment: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 36-574.

Mechanism of oxime reactivation of acetylcholinesterase analyzed by chirality and mutagenesis.
type: BibliographicResource
authors:
  item: Wong L
  item: Radic Z
  item: Bruggemann RJ
  item: Hosea N
  item: Berman HA
  item: Taylor P
journal: Biochemistry
pages: 5750-7
published year: 2000
volume: 39
references: http://www.ncbi.nlm.nih.gov/pubmed/10801325

Docking study of enantiomeric fonofos oxon bound to the active site of Torpedo californica acetylcholinesterase.
type: BibliographicResource
authors:
  item: Hirashima A
  item: Kuwano E
  item: Eto M
journal: Bioorg Med Chem
pages: 653-6
published year: 2000
volume: 8
references: http://www.ncbi.nlm.nih.gov/pubmed/10732982

Active-site gorge and buried water molecules in crystal structures of acetylcholinesterase from Torpedo californica.
type: BibliographicResource
authors:
  item: Koellner G
  item: Kryger G
  item: Millard CB
  item: Silman I
  item: Sussman JL
  item: Steiner T
journal: J Mol Biol
pages: 713-35
published year: 2000
volume: 296
references: http://www.ncbi.nlm.nih.gov/pubmed/10669619

Pathways of ligand clearance in acetylcholinesterase by multiple copy sampling.
type: BibliographicResource
authors:
  item: Van Belle D
  item: De Maria L
  item: Iurcu G
  item: Wodak SJ
journal: J Mol Biol
pages: 705-26
published year: 2000
volume: 298
references: http://www.ncbi.nlm.nih.gov/pubmed/10788331

Specific chemical and structural damage to proteins produced by synchrotron radiation.
type: BibliographicResource
authors:
  item: Weik M
  item: Sussman JL
  item: Ravelli RB
  item: Kryger G
  item: McSweeney S
  item: Raves ML
  item: Harel M
  item: Gros P
  item: Silman I
  item: Kroon J
journal: Proc Natl Acad Sci U S A
pages: 623-8
published year: 2000
volume: 97
references: http://www.ncbi.nlm.nih.gov/pubmed/10639129
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Molecular dynamics study of active-site interactions with tetracoordinate transients in acetylcholinesterase and its mutants.
type: BibliographicResource
authors:
  item: Enyedy IJ
  item: Kovach IM
  item: Bencsura A
journal: Biochem J
pages: 645-53
published year: 2001
volume: 353
references: http://www.ncbi.nlm.nih.gov/pubmed/11171062

Excavations into the active-site gorge of cholinesterases.
type: BibliographicResource
authors:
  item: Soreq H
  item: Gnatt A
  item: Loewenstein Y
  item: Neville LF
journal: Trends Biochem Sci
pages: 353-8
published year: 1992
volume: 17
references: http://www.ncbi.nlm.nih.gov/pubmed/1412713

A structural motif of acetylcholinesterase that promotes amyloid beta-peptide fibril formation.
type: BibliographicResource
authors:
  item: De Ferrari GV
  item: Canales MA
  item: Shin I
  item: Weiner LM
  item: Silman I
  item: Inestrosa NC
journal: Biochemistry
pages: 10447-57
published year: 2001
volume: 40
references: http://www.ncbi.nlm.nih.gov/pubmed/11523986

Does "butyrylization" of acetylcholinesterase through substitution of the six divergent aromatic amino acids in the active center gorge generate an enzyme mimic of butyrylcholinesterase?
type: BibliographicResource
authors:
  item: Kaplan D
  item: Ordentlich A
  item: Barak D
  item: Ariel N
  item: Kronman C
  item: Velan B
  item: Shafferman A
journal: Biochemistry
pages: 7433-45
published year: 2001
volume: 40
references: http://www.ncbi.nlm.nih.gov/pubmed/11412096

Short, strong hydrogen bonds at the active site of human acetylcholinesterase: proton NMR studies.
type: BibliographicResource
authors:
  item: Massiah MA
  item: Viragh C
  item: Reddy PM
  item: Kovach IM
  item: Johnson J
  item: Rosenberry TL
  item: Mildvan AS
journal: Biochemistry
pages: 5682-90
published year: 2001
volume: 40
references: http://www.ncbi.nlm.nih.gov/pubmed/11341833

A structure-based design approach to the development of novel, reversible AChE inhibitors.
type: BibliographicResource
authors:
  item: Doucet-Personeni C
  item: Viner R
  item: Silman I
  item: Sussman JL
  item: Greenblatt HM
  item: Lewis T
  item: Bentley PD
  item: Fletcher RJ
  item: Kinkaid A
  item: Kryger G
  item: Pirard B
  item: Taylor A
  item: Taylor R
  item: Taylor J
journal: J Med Chem
pages: 3203-15
published year: 2001
volume: 44
references: http://www.ncbi.nlm.nih.gov/pubmed/11563919
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Methyl analogues of the experimental Alzheimer drug phenserine: synthesis and structure/activity relationships for acetyl- and butyrylcholinesterase inhibitory action.
type: BibliographicResource
authors:
  item: Yu Q
  item: Holloway HW
  item: Flippen-Anderson JL
  item: Hoffman B
  item: Brossi A
  item: Greig NH
journal: J Med Chem
pages: 4062-71
published year: 2001
volume: 44
references: http://www.ncbi.nlm.nih.gov/pubmed/11708910

Accurate prediction of the bound conformation of galanthamine in the active site of Torpedo californica acetylcholinesterase using molecular docking.
type: BibliographicResource
authors:
  item: Pilger C
  item: Bartolucci C
  item: Lamba D
  item: Tropsha A
  item: Fels G
journal: J Mol Graph Model
pages: 288-96, 374-8
published year: 2001
volume: 19
references: http://www.ncbi.nlm.nih.gov/pubmed/11449566

Specific protein dynamics near the solvent glass transition assayed by radiation-induced structural changes.
type: BibliographicResource
authors:
  item: Weik M
  item: Ravelli RB
  item: Silman I
  item: Sussman JL
  item: Gros P
  item: Kroon J
journal: Protein Sci
pages: 1953-61
published year: 2001
volume: 10
references: http://www.ncbi.nlm.nih.gov/pubmed/11567086

Three-dimensional structure of a complex of galanthamine (Nivalin) with acetylcholinesterase from Torpedo californica: implications for the design of new anti-Alzheimer drugs.
type: BibliographicResource
authors:
  item: Bartolucci C
  item: Perola E
  item: Pilger C
  item: Fels G
  item: Lamba D
journal: Proteins
pages: 182-91
published year: 2001
volume: 42
references: http://www.ncbi.nlm.nih.gov/pubmed/11119642
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Molecular dynamics of acetylcholinesterase.
type: BibliographicResource
authors:
  item: Shen T
  item: Tai K
  item: Henchman RH
  item: McCammon JA
journal: Acc Chem Res
pages: 332-40
published year: 2002
volume: 35
references: http://www.ncbi.nlm.nih.gov/pubmed/12069617

Structure of a complex of the potent and specific inhibitor BW284C51 with Torpedo californica acetylcholinesterase.
type: BibliographicResource
authors:
  item: Felder CE
  item: Harel M
  item: Silman I
  item: Sussman JL
journal: Acta Crystallogr D Biol Crystallogr
pages: 1765-71
published year: 2002
volume: 58
references: http://www.ncbi.nlm.nih.gov/pubmed/12351819
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Three-dimensional structure of acetylcholinesterase and of its complexes with anticholinesterase drugs.
type: BibliographicResource
authors:
  item: Sussman JL
  item: Harel M
  item: Silman I
journal: Chem Biol Interact
pages: 187-97
published year: 1993
volume: 87
references: http://www.ncbi.nlm.nih.gov/pubmed/8343975

The aromatic "trapping" of the catalytic histidine is essential for efficient catalysis in acetylcholinesterase.
type: BibliographicResource
authors:
  item: Barak D
  item: Kaplan D
  item: Ordentlich A
  item: Ariel N
  item: Velan B
  item: Shafferman A
journal: Biochemistry
pages: 8245-52
published year: 2002
volume: 41
references: http://www.ncbi.nlm.nih.gov/pubmed/12081473

Kinetic and structural studies on the interaction of cholinesterases with the anti-Alzheimer drug rivastigmine.
type: BibliographicResource
authors:
  item: Bar-On P
  item: Millard CB
  item: Harel M
  item: Dvir H
  item: Enz A
  item: Sussman JL
  item: Silman I
journal: Biochemistry
pages: 3555-64
published year: 2002
volume: 41
references: http://www.ncbi.nlm.nih.gov/pubmed/11888271
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

X-ray structures of Torpedo californica acetylcholinesterase complexed with (+)-huperzine A and (-)-huperzine B: structural evidence for an active site rearrangement.
type: BibliographicResource
authors:
  item: Dvir H
  item: Silman I
  item: Bai DL
  item: Sussman JL
  item: Jiang HL
  item: Wong DM
  item: Harel M
  item: Chetrit M
  item: He XC
  item: Jin GY
  item: Yu GL
  item: Tang XC
journal: Biochemistry
pages: 10810-8
published year: 2002
volume: 41
references: http://www.ncbi.nlm.nih.gov/pubmed/12196020
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

3D structure of Torpedo californica acetylcholinesterase complexed with huprine X at 2.1 A resolution: kinetic and molecular dynamic correlates.
type: BibliographicResource
authors:
  item: Dvir H
  item: Silman I
  item: Sussman JL
  item: Wong DM
  item: Harel M
  item: Barril X
  item: Orozco M
  item: Luque FJ
  item: Munoz-Torrero D
  item: Camps P
  item: Rosenberry TL
journal: Biochemistry
pages: 2970-81
published year: 2002
volume: 41
references: http://www.ncbi.nlm.nih.gov/pubmed/11863435
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Substrate activation in acetylcholinesterase induced by low pH or mutation in the pi-cation subsite.
type: BibliographicResource
authors:
  item: Masson P
  item: Schopfer LM
  item: Bartels CF
  item: Froment MT
  item: Ribes F
  item: Nachon F
  item: Lockridge O
journal: Biochim Biophys Acta
pages: 313-24
published year: 2002
volume: 1594
references: http://www.ncbi.nlm.nih.gov/pubmed/11904227

Detection of unwanted protein-bound ligands by capillary zone electrophoresis: the case of hidden ligands that stabilize cholinesterase conformation.
type: BibliographicResource
authors:
  item: Rochu D
  item: Renault F
  item: Masson P
journal: Electrophoresis
pages: 930-7
published year: 2002
volume: 23
references: http://www.ncbi.nlm.nih.gov/pubmed/11920879

A neutral molecule in a cation-binding site: specific binding of a PEG-SH to acetylcholinesterase from Torpedo californica.
type: BibliographicResource
authors:
  item: Koellner G
  item: Steiner T
  item: Millard CB
  item: Silman I
  item: Sussman JL
journal: J Mol Biol
pages: 721-5
published year: 2002
volume: 320
references: http://www.ncbi.nlm.nih.gov/pubmed/12095250
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Unmasking tandem site interaction in human acetylcholinesterase. Substrate activation with a cationic acetanilide substrate.
type: BibliographicResource
authors:
  item: Johnson JL
  item: Cusack B
  item: Davies MP
  item: Fauq A
  item: Rosenberry TL
journal: Biochemistry
pages: 5438-52
published year: 2003
volume: 42
references: http://www.ncbi.nlm.nih.gov/pubmed/12731886

Acetylcholinesterase in motion: visualizing conformational changes in crystal structures by a morphing procedure.
type: BibliographicResource
authors:
  item: Zeev-Ben-Mordehai T
  item: Silman I
  item: Sussman JL
journal: Biopolymers
pages: 395-406
published year: 2003
volume: 68
references: http://www.ncbi.nlm.nih.gov/pubmed/12601798

Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site.
type: BibliographicResource
authors:
  item: Bourne Y
  item: Taylor P
  item: Radic Z
  item: Marchot P
journal: EMBO J
pages: 1-12
published year: 2003
volume: 22
references: http://www.ncbi.nlm.nih.gov/pubmed/12505979

Engineering resistance to 'aging' of phosphylated human acetylcholinesterase. Role of hydrogen bond network in the active center.
type: BibliographicResource
authors:
  item: Ordentlich A
  item: Kronman C
  item: Barak D
  item: Stein D
  item: Ariel N
  item: Marcus D
  item: Velan B
  item: Shafferman A
journal: FEBS Lett
pages: 215-20
published year: 1993
volume: 334
references: http://www.ncbi.nlm.nih.gov/pubmed/8224249

Aromatic amino-acid residues at the active and peripheral anionic sites control the binding of E2020 (Aricept) to cholinesterases.
type: BibliographicResource
authors:
  item: Saxena A
  item: Fedorko JM
  item: Vinayaka CR
  item: Medhekar R
  item: Radic Z
  item: Taylor P
  item: Lockridge O
  item: Doctor BP
journal: Eur J Biochem
pages: 4447-58
published year: 2003
volume: 270
references: http://www.ncbi.nlm.nih.gov/pubmed/14622273

Acetylcholinesterase complexed with bivalent ligands related to huperzine A: experimental evidence for species-dependent protein-ligand complementarity.
type: BibliographicResource
authors:
  item: Wong DM
  item: Greenblatt HM
  item: Dvir H
  item: Carlier PR
  item: Han YF
  item: Pang YP
  item: Silman I
  item: Sussman JL
journal: J Am Chem Soc
pages: 363-3
published year: 2003
volume: 125
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Nanosecond dynamics of the mouse acetylcholinesterase cys69-cys96 omega loop.
type: BibliographicResource
authors:
  item: Shi J
  item: Tai K
  item: McCammon JA
  item: Taylor P
  item: Johnson DA
journal: J Biol Chem
pages: 30905-11
published year: 2003
volume: 278
references: http://www.ncbi.nlm.nih.gov/pubmed/12759360

Molecular docking studies of natural cholinesterase-inhibiting steroidal alkaloids from Sarcococca saligna.
type: BibliographicResource
authors:
  item: Zaheer-Ul-Haq ZU
  item: Wellenzohn B
  item: Liedl KR
  item: Rode BM
journal: J Med Chem
pages: 5087-90
published year: 2003
volume: 46
references: http://www.ncbi.nlm.nih.gov/pubmed/14584959

Is aromaticity essential for trapping the catalytic histidine 447 in human acetylcholinesterase?
type: BibliographicResource
authors:
  item: Kaplan D
  item: Barak D
  item: Ordentlich A
  item: Kronman C
  item: Velan B
  item: Shafferman A
journal: Biochemistry
pages: 3129-36
published year: 2004
volume: 43
references: http://www.ncbi.nlm.nih.gov/pubmed/15023064

Nanosecond dynamics of acetylcholinesterase near the active center gorge.
type: BibliographicResource
authors:
  item: Boyd AE
  item: Dunlop CS
  item: Wong L
  item: Radic Z
  item: Taylor P
  item: Johnson DA
journal: J Biol Chem
pages: 26612-8
published year: 2004
volume: 279
references: http://www.ncbi.nlm.nih.gov/pubmed/15078872

A computational study of the binding of propidium to the peripheral anionic site of human acetylcholinesterase.
type: BibliographicResource
authors:
  item: Cavalli A
  item: Bottegoni G
  item: Raco C
  item: De Vivo M
  item: Recanatini M
journal: J Med Chem
pages: 3991-9
published year: 2004
volume: 47
references: http://www.ncbi.nlm.nih.gov/pubmed/15267237

The complex of a bivalent derivative of galanthamine with torpedo acetylcholinesterase displays drastic deformation of the active-site gorge: implications for structure-based drug design.
type: BibliographicResource
authors:
  item: Greenblatt HM
  item: Guillou C
  item: Guenard D
  item: Argaman A
  item: Botti S
  item: Badet B
  item: Thal C
  item: Silman I
  item: Sussman JL
journal: J Am Chem Soc
pages: 15405-11
published year: 2004
volume: 126
references: http://www.ncbi.nlm.nih.gov/pubmed/15563167
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Key active site residues in the inhibition of acetylcholinesterases by soman.
type: BibliographicResource
authors:
  item: Qian N
  item: Kovach IM
journal: FEBS Lett
pages: 263-6
published year: 1993
volume: 336
references: http://www.ncbi.nlm.nih.gov/pubmed/8262242

Quaternary ligand binding to aromatic residues in the active-site gorge of acetylcholinesterase.
type: BibliographicResource
authors:
  item: Harel M
  item: Schalk I
  item: Ehret-Sabatier L
  item: Bouet F
  item: Goeldner M
  item: Hirth C
  item: Axelsen PH
  item: Silman I
  item: Sussman JL
journal: Proc Natl Acad Sci U S A
pages: 9031-5
published year: 1993
volume: 90
references: http://www.ncbi.nlm.nih.gov/pubmed/8415649
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

1acjA
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 1acj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1acj

1aclA
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 1acl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1acl

1amnA
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 1amn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1amn

1ax9A
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 1ax9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ax9

1b41A
type: Pdb
catalytic residue: SER 203;GLU 334;HIS 447
main chain in catalysis: GLY 121;GLY 122;ALA 204
references: 1b41
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1b41

1cfjA
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 1cfj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cfj

1dx6A
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 1dx6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dx6

1e3qA
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 1e3q
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e3q

1e66A
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 1e66
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e66

1ea5A
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 1ea5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ea5

1eeaA
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 1eea
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1eea

1eveA
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 1eve
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1eve

1f8uA
type: Pdb
catalytic residue: SER 203;GLU 334;HIS 447
main chain in catalysis: GLY 121;GLY 122;ALA 204
references: 1f8u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f8u

1fssA
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 1fss
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fss

1gpkA
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 1gpk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gpk

1gpnA
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 1gpn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gpn

1gqrA
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 1gqr
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gqr

1gqsA
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 1gqs
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gqs

1h22A
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 1h22
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h22

1h23A
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 1h23
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h23

1hbjA
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 1hbj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hbj

1jjbA
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 1jjb
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jjb

1oceA
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 1oce
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1oce

1qidA
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 1qid
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qid

1qieA
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 1qie
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qie

1qifA
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 1qif
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qif

1qigA
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 1qig
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qig

1qihA
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 1qih
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qih

1qiiA
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 1qii
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qii

1qijA
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 1qij
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qij

1qikA
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 1qik
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qik

1qimA
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 1qim
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qim

1qtiA
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 1qti
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qti

1somA
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 1som
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1som

1votA
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 1vot
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vot

1vxoA
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 1vxo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vxo

1vxrA
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 1vxr
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vxr

1w4lA
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 1w4l
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1w4l

1w6rA
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 1w6r
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1w6r

1w75A
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 1w75
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1w75

1w75B
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 1w75
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1w75

1w76A
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 1w76
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1w76

1w76B
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 1w76
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1w76

2aceA
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 2ace
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2ace

2ackA
type: Pdb
catalytic residue: SER 200;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
references: 2ack
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2ack

2dfpA
type: Pdb
catalytic residue: ;GLU 327;HIS 440
main chain in catalysis: GLY 118;GLY 119;ALA 201
modified residue: MIS 200
references: 2dfp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2dfp
comment: Modified Ser200

Acetate
type: KeggProduct
compound type: carboxyl group
references: KEGG:C00033
references: CHEBI:15366
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Choline
type: KeggProduct
compound type: amine group
compound type: carbohydrate
references: KEGG:C00114
references: CHEBI:15354
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Acetylcholine
type: KeggSubstrate
compound type: amine group
compound type: carbohydrate
references: KEGG:C01996
references: CHEBI:15355
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Peptidyl-Ser-tetrahedral intermediate (with previous acetylcholine carboxylic-ester)
type: KeggIntermediate
references: KEGG:I00124

Acetyl-enzyme (Peptidyl-Ser-acetyl group)
type: KeggIntermediate
references: KEGG:I00125

Peptidyl-Ser-acetyl-tetrahedral-intermediate
type: KeggIntermediate
references: KEGG:I00126

true cholinesterase
type: KeggEnzyme

choline esterase I
type: KeggEnzyme

cholinesterase
type: KeggEnzyme

acetylthiocholinesterase
type: KeggEnzyme

acetylcholine hydrolase
type: KeggEnzyme

acetyl.beta-methylcholinesterase
type: KeggEnzyme

AcCholE
type: KeggEnzyme

Analogue
compound: Acetylcholine
ligand het code: DME
pdb: 1aclA

Analogue
compound: Choline
ligand het code: EDR
pdb: 1ax9A

Analogue
compound: Choline
ligand het code: GNT
pdb: 1dx6A

Analogue
compound: Choline
ligand het code: SAF
pdb: 1gqrA

Analogue
compound: Choline
ligand het code: SAF
pdb: 1gqsA

Analogue
compound: Choline
ligand het code: GNT
pdb: 1qtiA

Analogue
compound: Choline
ligand het code: GL8
pdb: 1w4lA

Analogue
compound: Choline
ligand het code: GNT
pdb: 1w6rA

Analogue
compound: Choline
ligand het code: GNT
pdb: 1w76A

Analogue
compound: Choline
ligand het code: GNT
pdb: 1w76B

Analogue
compound: Choline
ligand het code: EDR
pdb: 2ackA

TransitionStateAnalogue
compound: Peptidyl-Ser-tetrahedral intermediate (with previous acetylcholine carboxylic-ester)
ligand het code: NAF
pdb: 1amnA

TransitionStateAnalogue
compound: Peptidyl-Ser-tetrahedral intermediate (with previous acetylcholine carboxylic-ester)
ligand het code: _VX
pdb: 1vxrA

TransitionStateBound
compound: Peptidyl-Ser-tetrahedral intermediate (with previous acetylcholine carboxylic-ester)
ligand het code: ACH
pdb: 2aceA

IntermediateAnalogue
compound: Acetyl-enzyme (Peptidyl-Ser-acetyl group)
ligand het code: EMM
pdb: 1gqrA

IntermediateAnalogue
compound: Acetyl-enzyme (Peptidyl-Ser-acetyl group)
ligand het code: MF2
pdb: 1oceA

TransitionStateAnalogue
compound: Peptidyl-Ser-acetyl-tetrahedral-intermediate
ligand het code: _GB
pdb: 1cfjA

TransitionStateAnalogue
compound: Peptidyl-Ser-acetyl-tetrahedral-intermediate
ligand het code: FBQ
pdb: 1hbjA

TransitionStateAnalogue
compound: Peptidyl-Ser-acetyl-tetrahedral-intermediate
ligand het code: VXA
pdb: 1somA

TransitionStateAnalogue
compound: Peptidyl-Ser-acetyl-tetrahedral-intermediate
ligand het code: VXA
pdb: 1vxoA

TransitionStateAnalogue
compound: Peptidyl-Ser-acetyl-tetrahedral-intermediate
ligand het code: MIS
pdb: 2dfpA

ReferenceForCatalyticMechanism
reference index: 1
reference section: p.876-877

ReferenceForCatalyticMechanism
reference index: 8
reference section: Scheme 1

ReferenceForCatalyticMechanism
reference index: 20
reference section: p.838-839

ReferenceForCatalyticMechanism
reference index: 24
reference section: p.2324-2326

ReferenceForCatalyticMechanism
reference index: 36
reference section: Scheme 1

ReferenceForCatalyticMechanism
reference index: 52
reference section: Scheme 1, p.5683

ReferenceForCatalyticMechanism
reference index: 53
reference section: Fig.3