D00147
type: Enzyme
cath: Purple Acid Phosphatase; chain A, domain 2
cath: 5'-nucleotidase; domain 2
ec: https://purl.uniprot.org/enzyme/3.1.3.5
ec: https://purl.uniprot.org/enzyme/3.6.1.45
csa: 1ush
uniprot: P07024
kegg enzyme: 5'-nucleotidase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/3.1.3.5
kegg enzyme: uridine 5'-nucleotidase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/3.1.3.5
kegg enzyme: 5'-adenylic phosphatase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/3.1.3.5
kegg enzyme: adenosine 5'-phosphatase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/3.1.3.5
kegg enzyme: AMP phosphatase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/3.1.3.5
kegg enzyme: adenosine monophosphatase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/3.1.3.5
kegg enzyme: 5'-mononucleotidase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/3.1.3.5
kegg enzyme: AMPase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/3.1.3.5
kegg enzyme: UMPase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/3.1.3.5
kegg enzyme: snake venom 5'-nucleotidase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/3.1.3.5
kegg enzyme: thimidine monophosphate nucleotidase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/3.1.3.5
kegg enzyme: 5'-AMPase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/3.1.3.5
kegg enzyme: 5'-AMP nucleotidase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/3.1.3.5
kegg enzyme: AMP phosphohydrolase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/3.1.3.5
kegg enzyme: IMP 5'-nucleotidase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/3.1.3.5
kegg pathway: Purine metabolism
kegg pathway: Pyrimidine metabolism
kegg pathway: Nicotinate and nicotinamide metabolism
kegg cofactor: Zinc
kegg substrate: H2O
kegg substrate: 5'-Ribonucleotide
kegg substrate: UDP-sugar
kegg substrate: Nucleoside triphosphate
kegg substrate: Nucleoside diphosphate
kegg product: Ribonucleoside
kegg product: Phosphate
kegg product: UMP
kegg product: alpha-D-Aldose 1-phosphate
kegg product: Nucleoside diphosphate
kegg product: 5'-Ribonucleotide
pdb: 1ho5A01
pdb: 1ho5B01
pdb: 1hp1A01
pdb: 1hpuA01
pdb: 1hpuB01
pdb: 1hpuC01
pdb: 1hpuD01
pdb: 1oi8A01
pdb: 1oi8B01
pdb: 1oidA01
pdb: 1oidB01
pdb: 1oieA01
pdb: 1ushA01
pdb: 2ushA01
pdb: 2ushB01
pdb: 1ho5A02
pdb: 1ho5B02
pdb: 1hp1A02
pdb: 1hpuA02
pdb: 1hpuB02
pdb: 1hpuC02
pdb: 1hpuD02
pdb: 1oi8A02
pdb: 1oi8B02
pdb: 1oidA02
pdb: 1oidB02
pdb: 1oieA02
pdb: 1ushA02
pdb: 2ushA02
pdb: 2ushB02
active site residues resources: E. coli 5'-nucleotidase undergoes a hinge-bending domain rotation resembling a ball-and-socket motion.
active site residues resources: Cobalt activation of Escherichia coli 5'-nucleotidase is due to zinc ion displacement at only one of two metal-ion-binding sites.
references: Identification of histidyl and cysteinyl residues essential for catalysis by 5'-nucleotidase.
references: Kinetic characteristics of nucleoside mono-, di- and triphosphatase activities of the periplasmic 5'-nucleotidase of Escherichia coli.
references: X-ray structure of the Escherichia coli periplasmic 5'-nucleotidase containing a dimetal catalytic site.
references: E. coli 5'-nucleotidase undergoes a hinge-bending domain rotation resembling a ball-and-socket motion.
references: Mechanism of hydrolysis of phosphate esters by the dimetal center of 5'-nucleotidase based on crystal structures.
references: Cobalt activation of Escherichia coli 5'-nucleotidase is due to zinc ion displacement at only one of two metal-ion-binding sites.
references: Mammalian 5'-nucleotidases.
references: Trapping a 96 degrees domain rotation in two distinct conformations by engineered disulfide bridges.
references: A large hinge bending domain rotation is necessary for the catalytic function of Escherichia coli 5'-nucleotidase.
references: The catalytic mechanisms of binuclear metallohydrolases.
comment: According to the literature [2], this enzyme can hydrolyze nucleoside triphosphate (C00201) and nucleoside diphosphate (C00454) in addition to 5'-ribonucleotides (activity of EC 3.1.3.5) and UDP-sugars (activity of EC 3.6.1.45).

Purple Acid Phosphatase; chain A, domain 2
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.60.21.10
catalytic domain: index.html

5'-nucleotidase; domain 2
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.90.780.10
catalytic domain: index.html

Purine metabolism
type: KeggPathway
references: KEGG:MAP00230
ec: https://purl.uniprot.org/enzyme/3.1.3.5

Pyrimidine metabolism
type: KeggPathway
references: KEGG:MAP00240
ec: https://purl.uniprot.org/enzyme/3.1.3.5

Nicotinate and nicotinamide metabolism
type: KeggPathway
references: KEGG:MAP00760
ec: https://purl.uniprot.org/enzyme/3.1.3.5

Zinc
type: KeggCofactor
references: KEGG:C00038
references: CHEBI:29105
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: heavy metal

H2O
type: KeggSubstrate
references: KEGG:C00001
references: CHEBI:15377
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
ec: https://purl.uniprot.org/enzyme/3.1.3.5
ec: https://purl.uniprot.org/enzyme/3.6.1.45
compound type: H2O

5'-Ribonucleotide
type: KeggSubstrate
type: KeggProduct
references: KEGG:C02520
ec: https://purl.uniprot.org/enzyme/3.1.3.5
compound type: nucleotide

UDP-sugar
type: KeggSubstrate
references: KEGG:C05227
ec: https://purl.uniprot.org/enzyme/3.6.1.45
compound type: amide group
compound type: carbohydrate
compound type: nucleotide

Nucleoside triphosphate
type: KeggSubstrate
references: KEGG:C00201
compound type: nucleotide

Nucleoside diphosphate
type: KeggSubstrate
type: KeggProduct
references: KEGG:C00454
compound type: nucleotide

Ribonucleoside
type: KeggProduct
references: KEGG:C00911
ec: https://purl.uniprot.org/enzyme/3.1.3.5
compound type: nucleoside

Phosphate
type: KeggProduct
references: KEGG:C00009
references: CHEBI:26078
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
ec: https://purl.uniprot.org/enzyme/3.1.3.5
compound type: phosphate group/phosphate ion

UMP
type: KeggProduct
references: KEGG:C00105
references: CHEBI:16695
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
ec: https://purl.uniprot.org/enzyme/3.6.1.45
compound type: amide group
compound type: nucleotide

alpha-D-Aldose 1-phosphate
type: KeggProduct
references: KEGG:C00991
ec: https://purl.uniprot.org/enzyme/3.6.1.45
compound type: carbohydrate
compound type: phosphate group/phosphate ion

1ho5A01
type: Pdb
references: 1ho5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ho5
catalytic residue: ASN 116;HIS 117;ASP 120
cofactor binding residue: ASP 41;HIS 43;GLN 254(Zinc-1);ASP 84(Zinc-1 & 2);ASN 116;HIS 217;HIS 252(Zinc-2)

1ho5B01
type: Pdb
references: 1ho5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ho5
catalytic residue: ASN 116;HIS 117;ASP 120
cofactor binding residue: ASP 41;HIS 43;GLN 254(Zinc-1);ASP 84(Zinc-1 & 2);ASN 116;HIS 217;HIS 252(Zinc-2)

1hp1A01
type: Pdb
references: 1hp1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hp1
catalytic residue: ASN 116;HIS 117;ASP 120
cofactor binding residue: ASP 41;HIS 43;GLN 254(Zinc-1);ASP 84(Zinc-1 & 2);ASN 116;HIS 217;HIS 252(Zinc-2)

1hpuA01
type: Pdb
references: 1hpu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hpu
catalytic residue: ASN 116;HIS 117;ASP 120
cofactor binding residue: ASP 41;HIS 43;GLN 254(Zinc-1);ASP 84(Zinc-1 & 2);ASN 116;HIS 217;HIS 252(Zinc-2)

1hpuB01
type: Pdb
references: 1hpu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hpu
catalytic residue: ASN 116;HIS 117;ASP 120
cofactor binding residue: ASP 41;HIS 43;GLN 254(Zinc-1);ASP 84(Zinc-1 & 2);ASN 116;HIS 217;HIS 252(Zinc-2)

1hpuC01
type: Pdb
references: 1hpu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hpu
catalytic residue: ASN 116;HIS 117;ASP 120
cofactor binding residue: ASP 41;HIS 43;GLN 254(Zinc-1);ASP 84(Zinc-1 & 2);ASN 116;HIS 217;HIS 252(Zinc-2)

1hpuD01
type: Pdb
references: 1hpu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hpu
catalytic residue: ASN 116;HIS 117;ASP 120
cofactor binding residue: ASP 41;HIS 43;GLN 254(Zinc-1);ASP 84(Zinc-1 & 2);ASN 116;HIS 217;HIS 252(Zinc-2)

1oi8A01
type: Pdb
references: 1oi8
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1oi8
catalytic residue: ASN 116;HIS 117;ASP 120
cofactor binding residue: ASP 41;HIS 43;GLN 254(Zinc-1);ASP 84(Zinc-1 & 2);ASN 116;HIS 217;HIS 252(Zinc-2)
comment: mutant P90C, disulfide bridge(C90-C424)

1oi8B01
type: Pdb
references: 1oi8
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1oi8
catalytic residue: ASN 116;HIS 117;ASP 120
cofactor binding residue: ASP 41;HIS 43;GLN 254(Zinc-1);ASP 84(Zinc-1 & 2);ASN 116;HIS 217;HIS 252(Zinc-2)
comment: mutant P90C, disulfide bridge(C90-C424)

1oidA01
type: Pdb
references: 1oid
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1oid
catalytic residue: ASN 116;HIS 117;ASP 120
cofactor binding residue: ASP 41;HIS 43;GLN 254(Zinc-1);ASP 84(Zinc-1 & 2);ASN 116;HIS 217;HIS 252(Zinc-2)
comment: mutant S228C, disulfide bridge(C228-C513)

1oidB01
type: Pdb
references: 1oid
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1oid
catalytic residue: ASN 116;HIS 117;ASP 120
cofactor binding residue: ASP 41;HIS 43;GLN 254(Zinc-1);ASP 84(Zinc-1 & 2);ASN 116;HIS 217;HIS 252(Zinc-2)
comment: mutant S228C, disulfide bridge(C228-C513)

1oieA01
type: Pdb
references: 1oie
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1oie
catalytic residue: ASN 116;HIS 117;ASP 120
cofactor binding residue: ASP 41;HIS 43;GLN 254(Zinc-1);ASP 84(Zinc-1 & 2);ASN 116;HIS 217;HIS 252(Zinc-2)
comment: mutant S228C, disulfide bridge(C228-C513)

1ushA01
type: Pdb
references: 1ush
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ush
catalytic residue: ASN 116;HIS 117;ASP 120
cofactor binding residue: ASP 41;HIS 43;GLN 254(Zinc-1);ASP 84(Zinc-1 & 2);ASN 116;HIS 217;HIS 252(Zinc-2)

2ushA01
type: Pdb
references: 2ush
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2ush
catalytic residue: ASN 116;HIS 117;ASP 120
cofactor binding residue: ASP 41;HIS 43;GLN 254(Zinc-1);ASP 84(Zinc-1 & 2);ASN 116;HIS 217;HIS 252(Zinc-2)

2ushB01
type: Pdb
references: 2ush
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2ush
catalytic residue: ASN 116;HIS 117;ASP 120
cofactor binding residue: ASP 41;HIS 43;GLN 254(Zinc-1);ASP 84(Zinc-1 & 2);ASN 116;HIS 217;HIS 252(Zinc-2)

1ho5A02
type: Pdb
references: 1ho5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ho5
catalytic residue: ARG 375;ARG 379;ARG 410

1ho5B02
type: Pdb
references: 1ho5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ho5
catalytic residue: ARG 375;ARG 379;ARG 410

1hp1A02
type: Pdb
references: 1hp1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hp1
catalytic residue: ARG 375;ARG 379;ARG 410

1hpuA02
type: Pdb
references: 1hpu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hpu
catalytic residue: ARG 375;ARG 379;ARG 410

1hpuB02
type: Pdb
references: 1hpu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hpu
catalytic residue: ARG 375;ARG 379;ARG 410

1hpuC02
type: Pdb
references: 1hpu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hpu
catalytic residue: ARG 375;ARG 379;ARG 410

1hpuD02
type: Pdb
references: 1hpu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hpu
catalytic residue: ARG 375;ARG 379;ARG 410

1oi8A02
type: Pdb
references: 1oi8
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1oi8
catalytic residue: ARG 375;ARG 379;ARG 410
comment: mutant L424C, disulfide bridge C90-C424

1oi8B02
type: Pdb
references: 1oi8
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1oi8
catalytic residue: ARG 375;ARG 379;ARG 410
comment: mutant L424C, disulfide bridge C90-C424

1oidA02
type: Pdb
references: 1oid
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1oid
catalytic residue: ARG 375;ARG 379;ARG 410
comment: mutant P513C, disulfide bridge C228-C513

1oidB02
type: Pdb
references: 1oid
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1oid
catalytic residue: ARG 375;ARG 379;ARG 410
comment: mutant P513C, disulfide bridge C228-C513

1oieA02
type: Pdb
references: 1oie
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1oie
catalytic residue: ARG 375;ARG 379;ARG 410
comment: mutant P513C, disulfide bridge C228-C513

1ushA02
type: Pdb
references: 1ush
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ush
catalytic residue: ARG 375;ARG 379;ARG 410

2ushA02
type: Pdb
references: 2ush
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2ush
catalytic residue: ARG 375;ARG 379;ARG 410

2ushB02
type: Pdb
references: 2ush
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2ush
catalytic residue: ARG 375;ARG 379;ARG 410

E. coli 5'-nucleotidase undergoes a hinge-bending domain rotation resembling a ball-and-socket motion.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE.
references: http://www.ncbi.nlm.nih.gov/pubmed/11491294
references: P07024
journal: J Mol Biol
volume: 309
pages: 255-66
published year: 2001
authors:
  item: Knofel T
  item: Strater N

Cobalt activation of Escherichia coli 5'-nucleotidase is due to zinc ion displacement at only one of two metal-ion-binding sites.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12603203
journal: Biochem J
volume: 372
pages: 625-30
published year: 2003
authors:
  item: McMillen L
  item: Beacham IR
  item: Burns DM

Identification of histidyl and cysteinyl residues essential for catalysis by 5'-nucleotidase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6321242
journal: FEBS Lett
volume: 167
pages: 235-40
published year: 1984
authors:
  item: Worku Y
  item: Luzio JP
  item: Newby AC

Kinetic characteristics of nucleoside mono-, di- and triphosphatase activities of the periplasmic 5'-nucleotidase of Escherichia coli.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9180021
journal: Comp Biochem Physiol B Biochem Mol Biol
volume: 117
pages: 135-42
published year: 1997
authors:
  item: Garcia L
  item: Chayet L
  item: Kettlun AM
  item: Collados L
  item: Chiong M
  item: Traverso-Cori A
  item: Mancilla M
  item: Valenzuela MA

X-ray structure of the Escherichia coli periplasmic 5'-nucleotidase containing a dimetal catalytic site.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 26-550
medline id: 99260739
references: http://www.ncbi.nlm.nih.gov/pubmed/10331872
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P07024
journal: Nat Struct Biol
volume: 6
pages: 448-53
published year: 1999
authors:
  item: Knofel T
  item: Strater N

Mechanism of hydrolysis of phosphate esters by the dimetal center of 5'-nucleotidase based on crystal structures.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE; PRODUCT AND INHIBITOR.
references: http://www.ncbi.nlm.nih.gov/pubmed/11491293
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P07024
journal: J Mol Biol
volume: 309
pages: 239-54
published year: 2001
authors:
  item: Knofel T
  item: Strater N

Mammalian 5'-nucleotidases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12947102
journal: J Biol Chem
volume: 278
pages: 46195-8
published year: 2003
authors:
  item: Bianchi V
  item: Spychala J

Trapping a 96 degrees domain rotation in two distinct conformations by engineered disulfide bridges.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/15215524
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: Protein Sci
volume: 13
pages: 1811-22
published year: 2004
authors:
  item: Schultz-Heienbrok R
  item: Maier T
  item: Strater N

A large hinge bending domain rotation is necessary for the catalytic function of Escherichia coli 5'-nucleotidase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/15709736
journal: Biochemistry
volume: 44
pages: 2244-52
published year: 2005
authors:
  item: Schultz-Heienbrok R
  item: Maier T
  item: Strater N

The catalytic mechanisms of binuclear metallohydrolases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/16895331
journal: Chem Rev
volume: 106
pages: 3338-63
published year: 2006
authors:
  item: Mitic N
  item: Smith SJ
  item: Neves A
  item: Guddat LW
  item: Gahan LR
  item: Schenk G

UDP-sugar diphosphatase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.6.1.45

nucleosidediphosphate-sugar pyrophosphatase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.6.1.45

nucleosidediphosphate-sugar diphosphatase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.6.1.45

UDP-sugar hydrolase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.6.1.45

UDP-sugar pyrophosphatase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.6.1.45

Analogue
compound: Nucleoside diphosphate
pdb: 1hpuA02
ligand het code: A12

Analogue
compound: Nucleoside diphosphate
pdb: 1hpuB02
ligand het code: A12

Analogue
compound: Nucleoside diphosphate
pdb: 1hpuC02
ligand het code: A12

Analogue
compound: Nucleoside diphosphate
pdb: 1hpuD02
ligand het code: A12

Analogue
compound: Nucleoside diphosphate
pdb: 2ushA02
ligand het code: WO4_702-WO4_703

Analogue
compound: Zinc
pdb: 1ho5A01
ligand het code: 2x_MN

Analogue
compound: Zinc
pdb: 1ho5B01
ligand het code: 2x_MN

Analogue
compound: Zinc
pdb: 1hpuA01
ligand het code: 2x_MN

Analogue
compound: Zinc
pdb: 1hpuB01
ligand het code: 2x_MN

Analogue
compound: Zinc
pdb: 1hpuC01
ligand het code: 2x_MN

Analogue
compound: Zinc
pdb: 1hpuD01
ligand het code: 2x_MN

Analogue
compound: Zinc
pdb: 1oi8A01
ligand het code: 2x_MN

Analogue
compound: Zinc
pdb: 1oi8B01
ligand het code: 2x_MN

Analogue
compound: Zinc
pdb: 1oidA01
ligand het code: _NI

Analogue
compound: Zinc
pdb: 1oieA01
ligand het code: _NI

Analogue
compound: Phosphate
pdb: 1oi8A02
ligand het code: SO4

Analogue
compound: Phosphate
pdb: 1oi8B02
ligand het code: SO4

Analogue
compound: Phosphate
pdb: 1ushA02
ligand het code: SO4_603

Analogue
compound: Phosphate
pdb: 2ushB02
ligand het code: WO4_701

Analogue
compound: 5'-Ribonucleotide
pdb: 2ushB02
ligand het code: WO4_704

ReferenceForCatalyticMechanism
reference index: 1
reference section: Fig.4, p.239-240

ReferenceForCatalyticMechanism
reference index: 3
reference section: p.449-450, p.451-452

ReferenceForCatalyticMechanism
reference index: 5
reference section: Fig.8, p.249-252

ReferenceForCatalyticMechanism
reference index: 10
reference section: Fig.22, p.3357-3358