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1B59

COMPLEX OF HUMAN METHIONINE AMINOPEPTIDASE-2 COMPLEXED WITH OVALICIN

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0070006molecular_functionmetalloaminopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CO A 481
ChainResidue
AASP262
AHIS331
AGLU364
AGLU459
AOVA480
ACO482
AHOH695

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 482
ChainResidue
AASP262
AGLU459
ACO481
AHOH695
AASP251

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE OVA A 480
ChainResidue
AHIS231
ALEU328
AASN329
AHIS331
AILE338
AHIS339
ATYR444
ACO481
AHOH559
AHOH695

site_idIUM
Number of Residues1
DetailsTHE PROTEIN CONTAINS TWO METALS AT ITS ACTIVE SITE
ChainResidue
AHIS231

Functional Information from PROSITE/UniProt
site_idPS01202
Number of Residues17
DetailsMAP_2 Methionine aminopeptidase subfamily 2 signature. DIcKIDfGtHISGriiD
ChainResidueDetails
AASP246-ASP262

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000269|PubMed:16540317
ChainResidueDetails
AHIS231
AHIS339

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000269|PubMed:14534293, ECO:0000269|PubMed:16134930, ECO:0000269|PubMed:16540317, ECO:0000269|PubMed:17350258, ECO:0000269|PubMed:17636946
ChainResidueDetails
AASP251
AASP262
AHIS331
AGLU364
AGLU459

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a16
ChainResidueDetails
ALYS342
AGLU364

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a16
ChainResidueDetails
AGLU364

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PDB entries from 2024-07-17

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