Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2ADU

Human Methionine Aminopeptidase Complex with 4-Aryl-1,2,3-triazole Inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0070006molecular_functionmetalloaminopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 501
ChainResidue
AASP251
AASP262
AGLU459
ACO502
AR20906

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CO A 502
ChainResidue
ACO501
AR20906
AASP262
AHIS331
AGLU364
AGLU459

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE R20 A 906
ChainResidue
AHIS231
AASP251
AASP262
AHIS331
AHIS339
AGLU364
AHIS382
ATYR444
AGLU459
ACO501
ACO502
AHOH671

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

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon