D00441
type: Enzyme
active site residues resources: Domain flexibility in aspartic proteinases.
active site residues resources: P11838
cath: Cathepsin D, subunit A; domain 1
csa: 1eed
ec: https://purl.uniprot.org/enzyme/3.4.23.22
kegg enzyme: endothiapepsin
kegg intermediate: Amino-diol-tetrahedral intermediate
kegg product: Protein
kegg product: Peptide
kegg substrate: Protein
kegg substrate: Peptide
kegg substrate: H2O
pdb: 1e5oE01
pdb: 1e80E01
pdb: 1e81E01
pdb: 1e82E01
pdb: 1eedP01
pdb: 1entE01
pdb: 1eplE01
pdb: 1epmE01
pdb: 1epnE01
pdb: 1epoE01
pdb: 1eppE01
pdb: 1epqE01
pdb: 1eprE01
pdb: 1er8E01
pdb: 1gktA01
pdb: 1gvtA01
pdb: 1gvuA01
pdb: 1gvvA01
pdb: 1gvwA01
pdb: 1gvxA01
pdb: 1od1A01
pdb: 1oewA01
pdb: 1oexA01
pdb: 2er0E01
pdb: 2er6E01
pdb: 2er7E01
pdb: 2er9E01
pdb: 3er3E01
pdb: 3er5E01
pdb: 4apeA01
pdb: 4er1E01
pdb: 4er2E01
pdb: 4er4E01
pdb: 5er1E01
pdb: 5er2E01
pdb: 1e5oE02
pdb: 1e80E02
pdb: 1e81E02
pdb: 1e82E02
pdb: 1eedP02
pdb: 1entE02
pdb: 1eplE02
pdb: 1epmE02
pdb: 1epnE02
pdb: 1epoE02
pdb: 1eppE02
pdb: 1epqE02
pdb: 1eprE02
pdb: 1er8E02
pdb: 1gktA02
pdb: 1gvtA02
pdb: 1gvuA02
pdb: 1gvvA02
pdb: 1gvwA02
pdb: 1gvxA02
pdb: 1od1A02
pdb: 1oewA02
pdb: 1oexA02
pdb: 2er0E02
pdb: 2er6E02
pdb: 2er7E02
pdb: 2er9E02
pdb: 3er3E02
pdb: 3er5E02
pdb: 4apeA02
pdb: 4er1E02
pdb: 4er2E02

Analogue
compound: Peptide
ligand het code: 3AI
pdb: 1e5oE01

Analogue
compound: Peptide
ligand het code: DHI-PRO-PHE-HIS-LEU-LEU-VAL-TYR (chain I)
pdb: 1er8E01

Analogue
compound: Peptide
ligand het code: PRO-THR-GLU-PUK-ARG-GLU (chain I)
pdb: 1gvxA01

Analogue
compound: Peptide
ligand het code: PRO-THR-GLU-PHE-PUK-ARG-GLU (chain I)
pdb: 2er6E01

Analogue
compound: Peptide
ligand het code: PRO-HIS-PRO-PHE-HIS-LAV-ILE-HIS-LYS (chain I)
pdb: 4er4E01

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
ligand het code: 0GQ
pdb: 1e80E01

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
ligand het code: M91
pdb: 1e81E01

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
ligand het code: M90
pdb: 1e82E01

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
ligand het code: 0EO
pdb: 1eedP01

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
ligand het code: 0EM
pdb: 1entE01

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
ligand het code: PRO-LEU-GLU-PSA-ARG-LEU (chain I)
pdb: 1eplE01

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
ligand het code: THR-PHE-GLN-ALA-PSA-LEU-ARG-GLU (chain I)
pdb: 1epmE01

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
ligand het code: 2ZS
pdb: 1epnE01

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
ligand het code: 2Z3
pdb: 1epoE01

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
ligand het code: 1Z1
pdb: 1eppE01

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
ligand het code: 0QF
pdb: 1epqE01

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
ligand het code: 0QS
pdb: 1eprE01

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
ligand het code: BOC-HIS-PRO-PHE-HIS-LOV-ILE-HIS (chain B)
pdb: 1gktA01

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
ligand het code: 2ZS
pdb: 1gvtA01

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
ligand het code: PRO-PHE-HIS-STA-VAL-ILE (chain I)
pdb: 1gvuA01

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
ligand het code: 0GM
pdb: 1gvvA01

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
ligand het code: 0EM
pdb: 1gvwA01

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
ligand het code: 0QS
pdb: 1od1A01

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
ligand het code: BOC-HIS-PRO-PHE-ALA-LOV-ILE-HIS (chain B)
pdb: 1oexA01

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
ligand het code: IVA-HIS-PRO-PHE-HIS-CHS-LEU-PHE (chain I)
pdb: 2er0E01

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
ligand het code: BOC-HIS-PRO-PHE-HIS-LOV-ILE-HIS (chain I)
pdb: 2er7E01

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
ligand het code: BOC-HIS-PRO-PHE-HIS-STA-LEU-PHE (chain I)
pdb: 2er9E01

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
ligand het code: 0EL
pdb: 3er3E01

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
ligand het code: PRO-HIS-PRO-PHE-HIS-STA-VAL-ILE-HIS-LYS (chain I)
pdb: 3er5E01

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
ligand het code: 0ZP
pdb: 4er1E01

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
ligand het code: IVA-VAL-VAL-STA-ALA-STA (chain I)
pdb: 4er2E01

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
ligand het code: 0HT
pdb: 5er1E01

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
ligand het code: 0EK
pdb: 5er2E01

ReferenceForCatalyticMechanism
reference index: 6
reference section: Fig.3, p.11

ReferenceForCatalyticMechanism
reference index: 20
reference section: Fig.3, p.272

ReferenceForCatalyticMechanism
reference index: 24
reference section: Fig.4, p.325-326

ReferenceForCatalyticMechanism
reference index: 28
reference section: Fig.5

ReferenceForCatalyticMechanism
reference index: 29
reference section: Fig.2, Fig.7, Fig.8

ReferenceForCatalyticMechanism
reference index: 34
reference section: Fig.2, p.324

ReferenceForCatalyticMechanism
reference index: 39
reference section: Fig.1

ReferenceForCatalyticMechanism
reference index: 40
reference section: Fig.1

ReferenceForCatalyticMechanism
reference index: 41
reference section: Fig.2

ReferenceForCatalyticMechanism
reference index: 42
reference section: Fig.7

Cathepsin D, subunit A; domain 1
type: Cath
catalytic domain: index.html
references: http://www.cathdb.info/version/latest/superfamily/2.40.70.10

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

Homology among acid proteases: comparison of crystal structures at 3A resolution of acid proteases from Rhizopus chinensis and Endothia parasitica.
type: BibliographicResource
authors:
  item: Subramanian E
  item: Swan ID
  item: Liu M
  item: Davies DR
  item: Jenkins JA
  item: Tickle IJ
  item: Blundell TL
journal: Proc Natl Acad Sci U S A
medline id: 77148881
pages: 556-9
published year: 1977
volume: 74
references: http://www.ncbi.nlm.nih.gov/pubmed/322132
references: P11838
comment: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).

Theoretical calculations on the acidity of the active site in aspartic proteinases.
type: BibliographicResource
authors:
  item: Goldblum A
journal: Biochemistry
pages: 1653-8
published year: 1988
volume: 27
references: http://www.ncbi.nlm.nih.gov/pubmed/3284587

A Rational Approach to the Design of Antihypertensives. X-Ray Studies of Complexes between Aspartic Proteinases and Aminoalcohol Renin Inhibitors.
type: BibliographicResource
authors:
  item: Cooper
  item: C. J.
  item: Champness
  item: J. N
  item: J. B.
  item: Foundling
  item: S. I.
  item: Blundell
  item: T. L.
  item: Arrowsmith
  item: R. J.
  item: Harris
journal: Topics in Medicinal Chemistry
pages: 308-13
published year: 1988
volume: (Publisher:Royal Society Of Chemistry)
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

X-ray studies of aspartic proteinase-statine inhibitor complexes.
type: BibliographicResource
authors:
  item: Cooper JB
  item: Foundling SI
  item: Blundell TL
  item: Boger J
  item: Jupp RA
  item: Kay J
journal: Biochemistry
pages: 8596-603
published year: 1989
volume: 28
references: http://www.ncbi.nlm.nih.gov/pubmed/2690945
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

http://ezcatdb.cbrc.jp/EzCatDB/reference/D00441#13
type: BibliographicResource
title: High-resolution X-ray diffraction study of the complex between endothiapepsin and an oligopeptide inhibitor: the analysis of the inhibitor binding and description of the rigid body shift in the enzyme.
authors:
  item: Sali A
  item: Veerapandian B
  item: Cooper JB
  item: Foundling SI
  item: Hoover DJ
  item: Blundell TL
journal: EMBO J
medline id: 90005421
pages: 2179-88
published year: 1989
volume: 8
references: http://www.ncbi.nlm.nih.gov/pubmed/2676515
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P11838
comment: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

Comparative X-ray crystallographic evidence for a beta-bend conformation as the active structure for peptide T in T4 receptor recognition.
type: BibliographicResource
authors:
  item: Chen J
  item: Barber A
  item: Pedersen J
  item: Brandt-Rauf PW
  item: Carucci J
  item: Murphy RB
  item: Carty RP
  item: Licht D
  item: Pincus MR
journal: J Protein Chem
pages: 87-100
published year: 1989
volume: 8
references: http://www.ncbi.nlm.nih.gov/pubmed/2548525

Modulation of the affinity of aspartic proteases by the mutated residues in active site models.
type: BibliographicResource
authors:
  item: Goldblum A
journal: FEBS Lett
pages: 241-4
published year: 1990
volume: 261
references: http://www.ncbi.nlm.nih.gov/pubmed/2107098

X-ray analyses of aspartic proteinases. The three-dimensional structure at 2.1 A resolution of endothiapepsin.
type: BibliographicResource
authors:
  item: Blundell TL
  item: Jenkins JA
  item: Sewell BT
  item: Pearl LH
  item: Cooper JB
  item: Tickle IJ
  item: Veerapandian B
  item: Wood SP
journal: J Mol Biol
medline id: 90189152
pages: 919-41
published year: 1990
volume: 211
references: http://www.ncbi.nlm.nih.gov/pubmed/2179568
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P11838
comment: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).

Molecular and crystal structures of monoclinic porcine pepsin refined at 1.8 A resolution.
type: BibliographicResource
authors:
  item: Sielecki AR
  item: Fedorov AA
  item: Boodhoo A
  item: Andreeva NS
  item: James MN
journal: J Mol Biol
pages: 143-70
published year: 1990
volume: 214
references: http://www.ncbi.nlm.nih.gov/pubmed/2115087

X-ray analyses of aspartic proteinases. III Three-dimensional structure of endothiapepsin complexed with a transition-state isostere inhibitor of renin at 1.6 A resolution.
type: BibliographicResource
authors:
  item: Veerapandian B
  item: Cooper JB
  item: Sali A
  item: Blundell TL
journal: J Mol Biol
pages: 1017-29
published year: 1990
volume: 216
references: http://www.ncbi.nlm.nih.gov/pubmed/2266553
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Revised 2.3 A structure of porcine pepsin: evidence for a flexible subdomain.
type: BibliographicResource
authors:
  item: Abad-Zapatero C
  item: Rydel TJ
  item: Erickson J
journal: Proteins
pages: 62-81
published year: 1990
volume: 8
references: http://www.ncbi.nlm.nih.gov/pubmed/2217165

The active site of aspartic proteinases.
type: BibliographicResource
authors:
  item: Pearl L
  item: Blundell T
journal: FEBS Lett
pages: 96-101
published year: 1984
volume: 174
references: http://www.ncbi.nlm.nih.gov/pubmed/6381096
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

X-ray analysis of a difluorostatone renin inhibitor bound as the tetrahedral hydrate to the aspartic protease endothiapepsin.
type: BibliographicResource
authors:
  item: Hoover DJ
  item: Veerapandian B
  item: Cooper JB
  item: Damon DB
  item: Dominy BW
  item: Rosati RL
  item: Blundell TL
journal: Adv Exp Med Biol
pages: 269-73
published year: 1991
volume: 306
references: http://www.ncbi.nlm.nih.gov/pubmed/1812716

A kinetic and equilibrium study of the denaturation of aspartic proteinases from the fungi, Endothia parasitica and Mucor miehei.
type: BibliographicResource
authors:
  item: Brown ED
  item: Yada RY
journal: Biochim Biophys Acta
pages: 406-15
published year: 1991
volume: 1076
references: http://www.ncbi.nlm.nih.gov/pubmed/2001389

X-ray crystallographic analysis of inhibition of endothiapepsin by cyclohexyl renin inhibitors.
type: BibliographicResource
authors:
  item: Cooper J
  item: Quail W
  item: Frazao C
  item: Foundling SI
  item: Blundell TL
  item: Humblet C
  item: Lunney EA
  item: Lowther WT
  item: Dunn BM
journal: Biochemistry
pages: 8142-50
published year: 1992
volume: 31
references: http://www.ncbi.nlm.nih.gov/pubmed/1525155
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Synthesis and crystallographic analysis of two rhizopuspepsin inhibitor complexes.
type: BibliographicResource
authors:
  item: Parris KD
  item: Hoover DJ
  item: Damon DB
  item: Davies DR
journal: Biochemistry
pages: 8125-41
published year: 1992
volume: 31
references: http://www.ncbi.nlm.nih.gov/pubmed/1525154

Direct observation by X-ray analysis of the tetrahedral "intermediate" of aspartic proteinases.
type: BibliographicResource
authors:
  item: Veerapandian B
  item: Cooper JB
  item: Sali A
  item: Blundell TL
  item: Rosati RL
  item: Dominy BW
  item: Damon DB
  item: Hoover DJ
journal: Protein Sci
pages: 322-8
published year: 1992
volume: 1
references: http://www.ncbi.nlm.nih.gov/pubmed/1304340
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Secondary substrate binding in aspartic proteinases: contributions of subsites S3 and S'2 to kcat.
type: BibliographicResource
authors:
  item: Balbaa M
  item: Cunningham A
  item: Hofmann T
journal: Arch Biochem Biophys
pages: 297-303
published year: 1993
volume: 306
references: http://www.ncbi.nlm.nih.gov/pubmed/8215428

X-ray-crystallographic studies of complexes of pepstatin A and a statine-containing human renin inhibitor with endothiapepsin.
type: BibliographicResource
authors:
  item: Bailey D
  item: Cooper JB
  item: Veerapandian B
  item: Blundell TL
  item: Atrash B
  item: Jones DM
  item: Szelke M
journal: Biochem J
pages: 363-71
published year: 1993
volume: 289
references: http://www.ncbi.nlm.nih.gov/pubmed/8424781

A quantum mechanical study of the active site of aspartic proteinases.
type: BibliographicResource
authors:
  item: Beveridge AJ
  item: Heywood GC
journal: Biochemistry
pages: 3325-33
published year: 1993
volume: 32
references: http://www.ncbi.nlm.nih.gov/pubmed/8461297

Extending crystallographic information with semiempirical quantum mechanics and molecular mechanics: a case of aspartic proteinases.
type: BibliographicResource
authors:
  item: Goldblum A
  item: Rayan A
  item: Fliess A
  item: Glick M
journal: J Chem Inf Comput Sci
pages: 270-4
published year: 1993
volume: 33
references: http://www.ncbi.nlm.nih.gov/pubmed/8391019

Energy calculations on aspartic proteinases: human renin, endothiapepsin and its complex with an angiotensinogen fragment analogue, H-142.
type: BibliographicResource
authors:
  item: Hemmings AM
  item: Foundling SI
  item: Sibanda BL
  item: Wood SP
  item: Pearl LH
  item: Blundell T
journal: Biochem Soc Trans
pages: 1036-41
published year: 1985
volume: 13
references: http://www.ncbi.nlm.nih.gov/pubmed/3912234

On the prediction of binding properties of drug molecules by comparative molecular field analysis.
type: BibliographicResource
authors:
  item: Klebe G
  item: Abraham U
journal: J Med Chem
pages: 70-80
published year: 1993
volume: 36
references: http://www.ncbi.nlm.nih.gov/pubmed/8380615

Analyses of ligand binding in five endothiapepsin crystal complexes and their use in the design and evaluation of novel renin inhibitors.
type: BibliographicResource
authors:
  item: Lunney EA
  item: Lowther WT
  item: et al
  item: Hamilton HW
  item: Hodges JC
  item: Kaltenbronn JS
  item: Repine JT
  item: Badasso M
  item: Cooper JB
  item: Dealwis C
  item: Wallace BA
journal: J Med Chem
pages: 3809-20
published year: 1993
volume: 36
references: http://www.ncbi.nlm.nih.gov/pubmed/8254610
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

A structural comparison of 21 inhibitor complexes of the aspartic proteinase from Endothia parasitica.
type: BibliographicResource
authors:
  item: Bailey D
  item: Cooper JB
journal: Protein Sci
pages: 2129-43
published year: 1994
volume: 3
references: http://www.ncbi.nlm.nih.gov/pubmed/7703859
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Thermodynamic mapping of the inhibitor site of the aspartic protease endothiapepsin.
type: BibliographicResource
authors:
  item: Gomez J
  item: Freire E
journal: J Mol Biol
pages: 337-50
published year: 1995
volume: 252
references: http://www.ncbi.nlm.nih.gov/pubmed/7563055

A theoretical study of torsional flexibility in the active site of aspartic proteinases: implications for catalysis.
type: BibliographicResource
authors:
  item: Beveridge A
journal: Proteins
pages: 322-34
published year: 1996
volume: 24
references: http://www.ncbi.nlm.nih.gov/pubmed/8778779

The three-dimensional structure at 2.4 A resolution of glycosylated proteinase A from the lysosome-like vacuole of Saccharomyces cerevisiae.
type: BibliographicResource
authors:
  item: Aguilar CF
  item: Blundell TL
  item: Cronin NB
  item: Badasso M
  item: Dreyer T
  item: Newman MP
  item: Cooper JB
  item: Hoover DJ
  item: Wood SP
  item: Johnson MS
journal: J Mol Biol
pages: 899-915
published year: 1997
volume: 267
references: http://www.ncbi.nlm.nih.gov/pubmed/9135120

A fast estimate of electrostatic group contributions to the free energy of protein-inhibitor binding.
type: BibliographicResource
authors:
  item: Muegge I
  item: Tao H
  item: Warshel A
journal: Protein Eng
pages: 1363-72
published year: 1997
volume: 10
references: http://www.ncbi.nlm.nih.gov/pubmed/9542997

Refinement of Four Endothiapepsin Inhibitor Complexes. Crystallographic Studies of Cytochrome Ch from Methylobacterium Extorquens and Inhibitor Complexes of Aspartic Proteinases.
type: BibliographicResource
authors:
  item: Read JA
journal: Crystallographic Studies
pages: 237 leaves
published year: 1999
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography (Ph D Thesis 1999 London University Birkbeck College)

Dynamic ligand design and combinatorial optimization: designing inhibitors to endothiapepsin.
type: BibliographicResource
authors:
  item: Stultz CM
  item: Karplus M
journal: Proteins
pages: 258-89
published year: 2000
volume: 40
references: http://www.ncbi.nlm.nih.gov/pubmed/10842341

A neutron Laue diffraction study of endothiapepsin: implications for the aspartic proteinase mechanism.
type: BibliographicResource
authors:
  item: Coates L
  item: Erskine PT
  item: Wood SP
  item: Myles DA
  item: Cooper JB
journal: Biochemistry
pages: 13149-57
published year: 2001
volume: 40
references: http://www.ncbi.nlm.nih.gov/pubmed/11683623
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: Neutron diffraction

http://ezcatdb.cbrc.jp/EzCatDB/reference/D00441#4
type: BibliographicResource
title: The pH dependence of the hydrolysis of chromogenic substrates of the type, Lys-Pro-Xaa-Yaa-Phe-(NO2)Phe-Arg-Leu, by selected aspartic proteinases: evidence for specific interactions in subsites S3 and S2.
authors:
  item: Dunn BM
  item: Valler MJ
  item: Rolph CE
  item: Foundling SI
  item: Jimenez M
  item: Kay J
journal: Biochim Biophys Acta
pages: 122-30
published year: 1987
volume: 913
references: http://www.ncbi.nlm.nih.gov/pubmed/3109484

Five atomic resolution structures of endothiapepsin inhibitor complexes: implications for the aspartic proteinase mechanism.
type: BibliographicResource
authors:
  item: Coates L
  item: Erskine PT
  item: Crump MP
  item: Wood SP
  item: Cooper JB
journal: J Mol Biol
pages: 1405-15
published year: 2002
volume: 318
references: http://www.ncbi.nlm.nih.gov/pubmed/12083527
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

The structure of endothiapepsin complexed with the gem-diol inhibitor PD-135,040 at 1.37 A.
type: BibliographicResource
authors:
  item: Coates L
  item: Erskine PT
  item: Mall S
  item: Williams PA
  item: Gill RS
  item: Wood SP
  item: Cooper JB
journal: Acta Crystallogr D Biol Crystallogr
pages: 978-81
published year: 2003
volume: 59
references: http://www.ncbi.nlm.nih.gov/pubmed/12777758
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Atomic resolution analysis of the catalytic site of an aspartic proteinase and an unexpected mode of binding by short peptides.
type: BibliographicResource
authors:
  item: Erskine PT
  item: Coates L
  item: Mall S
  item: Gill RS
  item: Wood SP
  item: Myles DA
  item: Cooper JB
journal: Protein Sci
pages: 1741-9
published year: 2003
volume: 12
references: http://www.ncbi.nlm.nih.gov/pubmed/12876323
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

http://ezcatdb.cbrc.jp/EzCatDB/reference/D00441#43
type: BibliographicResource
title: Calculating proton uptake/release and binding free energy taking into account ionization and conformation changes induced by protein-inhibitor association: application to plasmepsin, cathepsin D and endothiapepsin-pepstatin complexes.
authors:
  item: Alexov E
journal: Proteins
pages: 572-84
published year: 2004
volume: 56
references: http://www.ncbi.nlm.nih.gov/pubmed/15229889

The structure of a synthetic pepsin inhibitor complexed with endothiapepsin.
type: BibliographicResource
authors:
  item: Cooper J
  item: Foundling S
  item: Hemmings A
  item: Blundell T
  item: Jones DM
  item: Hallett A
  item: Szelke M
journal: Eur J Biochem
pages: 215-21
published year: 1987
volume: 169
references: http://www.ncbi.nlm.nih.gov/pubmed/3119339
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

The catalytic mechanism of aspartic proteinases.
type: BibliographicResource
authors:
  item: Pearl LH
journal: FEBS Lett
pages: 8-12
published year: 1987
volume: 214
references: http://www.ncbi.nlm.nih.gov/pubmed/3552727

Crystallographic studies of reduced bond inhibitors complexed with an aspartic proteinase.
type: BibliographicResource
authors:
  item: Foundling SI
  item: Sueiras J
  item: et al
  item: Cooper J
  item: Watson FE
  item: Pearl LH
  item: Hemmings A
  item: Wood SP
  item: Blundell T
  item: Hallett A
  item: Jones DM
journal: J Cardiovasc Pharmacol
pages: S59-68
published year: 1987
volume: 10 Suppl 7
references: http://www.ncbi.nlm.nih.gov/pubmed/2485065

Evolution in the structure and function of aspartic proteases.
type: BibliographicResource
authors:
  item: Tang J
  item: Wong RN
journal: J Cell Biochem
pages: 53-63
published year: 1987
volume: 33
references: http://www.ncbi.nlm.nih.gov/pubmed/3546346

High resolution X-ray analyses of renin inhibitor-aspartic proteinase complexes.
type: BibliographicResource
authors:
  item: Foundling SI
  item: Valler MJ
  item: et al
  item: Cooper J
  item: Watson FE
  item: Cleasby A
  item: Pearl LH
  item: Sibanda BL
  item: Hemmings A
  item: Wood SP
  item: Blundell TL
journal: Nature
pages: 349-52
published year: 1987
volume: 327
references: http://www.ncbi.nlm.nih.gov/pubmed/3295561
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Domain flexibility in aspartic proteinases.
type: BibliographicResource
authors:
  item: Sali A
  item: Veerapandian B
  item: Cooper JB
  item: Moss DS
  item: Hofmann T
  item: Blundell TL
journal: Proteins
pages: 158-70
published year: 1992
volume: 12
references: http://www.ncbi.nlm.nih.gov/pubmed/1603805

1oewA01
type: Pdb
catalytic residue: ASP 35
references: 1oew
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1oew

1e5oE01
type: Pdb
catalytic residue: ASP 32
references: 1e5o
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e5o

1e5oE02
type: Pdb
catalytic residue: ASP 215
references: 1e5o
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e5o

1e80E01
type: Pdb
catalytic residue: ASP 32
references: 1e80
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e80

1e80E02
type: Pdb
catalytic residue: ASP 215
references: 1e80
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e80

1e81E01
type: Pdb
catalytic residue: ASP 32
references: 1e81
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e81

1e81E02
type: Pdb
catalytic residue: ASP 215
references: 1e81
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e81

1e82E01
type: Pdb
catalytic residue: ASP 32
references: 1e82
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e82

1e82E02
type: Pdb
catalytic residue: ASP 215
references: 1e82
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e82

1eedP01
type: Pdb
catalytic residue: ASP 32
references: 1eed
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1eed

1eedP02
type: Pdb
catalytic residue: ASP 215
references: 1eed
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1eed

1entE01
type: Pdb
catalytic residue: ASP 32
references: 1ent
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ent

1entE02
type: Pdb
catalytic residue: ASP 215
references: 1ent
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ent

1eplE01
type: Pdb
catalytic residue: ASP 32
references: 1epl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1epl

1eplE02
type: Pdb
catalytic residue: ASP 215
references: 1epl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1epl

1epmE01
type: Pdb
catalytic residue: ASP 32
references: 1epm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1epm

1epmE02
type: Pdb
catalytic residue: ASP 215
references: 1epm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1epm

1epnE01
type: Pdb
catalytic residue: ASP 32
references: 1epn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1epn

1epnE02
type: Pdb
catalytic residue: ASP 215
references: 1epn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1epn

1epoE01
type: Pdb
catalytic residue: ASP 32
references: 1epo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1epo

1epoE02
type: Pdb
catalytic residue: ASP 215
references: 1epo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1epo

1eppE01
type: Pdb
catalytic residue: ASP 32
references: 1epp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1epp

1eppE02
type: Pdb
catalytic residue: ASP 215
references: 1epp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1epp

1epqE01
type: Pdb
catalytic residue: ASP 32
references: 1epq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1epq

1epqE02
type: Pdb
catalytic residue: ASP 215
references: 1epq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1epq

1eprE01
type: Pdb
catalytic residue: ASP 32
references: 1epr
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1epr

1eprE02
type: Pdb
catalytic residue: ASP 215
references: 1epr
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1epr

1er8E01
type: Pdb
catalytic residue: ASP 32
references: 1er8
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1er8

1er8E02
type: Pdb
catalytic residue: ASP 215
references: 1er8
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1er8

1gktA01
type: Pdb
catalytic residue: ASP 35
references: 1gkt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gkt

1gktA02
type: Pdb
catalytic residue: ASP 219
references: 1gkt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gkt

1gvtA01
type: Pdb
catalytic residue: ASP 35
references: 1gvt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gvt

1gvtA02
type: Pdb
catalytic residue: ASP 219
references: 1gvt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gvt

1gvuA01
type: Pdb
catalytic residue: ASP 35
references: 1gvu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gvu

1gvuA02
type: Pdb
catalytic residue: ASP 219
references: 1gvu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gvu

1gvvA01
type: Pdb
catalytic residue: ASP 35
references: 1gvv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gvv

1gvvA02
type: Pdb
catalytic residue: ASP 219
references: 1gvv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gvv

1gvwA01
type: Pdb
catalytic residue: ASP 35
references: 1gvw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gvw

1gvwA02
type: Pdb
catalytic residue: ASP 219
references: 1gvw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gvw

1gvxA01
type: Pdb
catalytic residue: ASP 35
references: 1gvx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gvx

1gvxA02
type: Pdb
catalytic residue: ASP 219
references: 1gvx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gvx

1od1A01
type: Pdb
catalytic residue: ASP 35
references: 1od1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1od1

1od1A02
type: Pdb
catalytic residue: ASP 219
references: 1od1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1od1

1oewA02
type: Pdb
catalytic residue: ASP 218
references: 1oew
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1oew

1oexA01
type: Pdb
catalytic residue: ASP 35
references: 1oex
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1oex

1oexA02
type: Pdb
catalytic residue: ASP 218
references: 1oex
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1oex

2er0E01
type: Pdb
catalytic residue: ASP 32
references: 2er0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2er0

2er0E02
type: Pdb
catalytic residue: ASP 215
references: 2er0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2er0

2er6E01
type: Pdb
catalytic residue: ASP 32
references: 2er6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2er6

2er6E02
type: Pdb
catalytic residue: ASP 215
references: 2er6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2er6

2er7E01
type: Pdb
catalytic residue: ASP 32
references: 2er7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2er7

2er7E02
type: Pdb
catalytic residue: ASP 215
references: 2er7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2er7

2er9E01
type: Pdb
catalytic residue: ASP 32
references: 2er9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2er9

2er9E02
type: Pdb
catalytic residue: ASP 215
references: 2er9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2er9

3er3E01
type: Pdb
catalytic residue: ASP 32
references: 3er3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3er3

3er3E02
type: Pdb
catalytic residue: ASP 215
references: 3er3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3er3

3er5E01
type: Pdb
catalytic residue: ASP 32
references: 3er5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3er5

3er5E02
type: Pdb
catalytic residue: ASP 215
references: 3er5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3er5

4apeA01
type: Pdb
catalytic residue: ASP 32
references: 4ape
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4ape

4apeA02
type: Pdb
catalytic residue: ASP 215
references: 4ape
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4ape

4er1E01
type: Pdb
catalytic residue: ASP 32
references: 4er1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4er1

4er1E02
type: Pdb
catalytic residue: ASP 215
references: 4er1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4er1

4er2E01
type: Pdb
catalytic residue: ASP 32
references: 4er2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4er2

4er2E02
type: Pdb
catalytic residue: ASP 215
references: 4er2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4er2

4er4E01
type: Pdb
catalytic residue: ASP 32
references: 4er4
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4er4

4er4E02
type: Pdb
catalytic residue: ASP 215
references: 4er4
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4er4

5er1E01
type: Pdb
catalytic residue: ASP 32
references: 5er1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:5er1

5er1E02
type: Pdb
catalytic residue: ASP 215
references: 5er1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:5er1

5er2E01
type: Pdb
catalytic residue: ASP 32
references: 5er2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:5er2

5er2E02
type: Pdb
catalytic residue: ASP 215
references: 5er2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:5er2

Amino-diol-tetrahedral intermediate
type: KeggIntermediate
references: KEGG:I00136

Peptide
type: KeggSubstrate
type: KeggProduct
compound type: peptide/protein
references: KEGG:C00012

Protein
type: KeggSubstrate
type: KeggProduct
compound type: peptide/protein
references: KEGG:C00017

Endothia aspartic proteinase
type: KeggEnzyme

Endothia acid proteinase
type: KeggEnzyme

Endothia parasitica acid proteinase
type: KeggEnzyme

Endothia parasitica aspartic proteinase
type: KeggEnzyme