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5D6E

Structure of human methionine aminopeptidase 2 with covalent spiroepoxytriazole inhibitor (-)-31b

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0070006molecular_functionmetalloaminopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues19
Detailsbinding site for residue 94A A 501
ChainResidue
AHIS231
AHIS382
AALA414
ATYR444
AGLU459
ACO502
ACO503
AHOH633
AHOH655
AHOH852
AHOH861
AASP262
AASN327
ALEU328
AASN329
AHIS331
AILE338
AHIS339
AGLU364

site_idAC2
Number of Residues6
Detailsbinding site for residue CO A 502
ChainResidue
AASP251
AASP262
AGLU459
A94A501
ACO503
AHOH655

site_idAC3
Number of Residues7
Detailsbinding site for residue CO A 503
ChainResidue
AASP262
AHIS331
AGLU364
AGLU459
A94A501
ACO502
AHOH655

site_idAC4
Number of Residues3
Detailsbinding site for residue TBU A 504
ChainResidue
ATHR268
APHE269
AHOH615

site_idAC5
Number of Residues5
Detailsbinding site for residue TBU A 505
ChainResidue
APRO189
APRO189
ATYR244
ATYR244
AHOH778

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 2024-07-10

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