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6QEH

CRYSTAL STRUCTURE OF HUMAN METHIONINE AMINOPEPTIDASE-2 IN COMPLEX WITH AN INHIBITOR 5-Chloro-quinolin-8-ol

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0070006molecular_functionmetalloaminopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue GOL A 501
ChainResidue
AARG180
AHIS460
AARG474

site_idAC2
Number of Residues10
Detailsbinding site for residue HZQ A 502
ChainResidue
AGLU459
AMN503
AMN504
AHOH725
APHE219
AHIS231
AASP251
AASP262
AHIS331
AGLU364

site_idAC3
Number of Residues6
Detailsbinding site for residue MN A 503
ChainResidue
AASP262
AHIS331
AGLU364
AGLU459
AHZQ502
AMN504

site_idAC4
Number of Residues6
Detailsbinding site for residue MN A 504
ChainResidue
APHE219
AASP251
AASP262
AGLU459
AHZQ502
AMN503

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

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PDB entries from 2024-09-11

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