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

2G6P

Crystal structure of truncated (delta 1-89) human methionine aminopeptidase Type 1 in complex with Pyridyl pyrimidine derivative

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 401
ChainResidue
AASP240
AHIS303
ATHR334
AGLU336
AGLU367
ACO402
AHOH624

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CO A 402
ChainResidue
AGLU367
ACO401
AHOH514
AHOH624
AASP229
AASP240

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 403
ChainResidue
AHIS212
AHM2410
AHOH500
AHOH501
AHOH502

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K A 404
ChainResidue
ASER205
AVAL206
AASN207
AVAL209
ASER363
AHOH531

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE HM2 A 410
ChainResidue
ATYR195
ACYS203
AHIS212
AHIS310
ATRP353
ACO403
AEPE471

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EPE A 471
ChainResidue
ATYR196
AGLY352
ATRP353
AHM2410

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 470
ChainResidue
ATHR172
ATHR204
ASER205
AVAL206
AVAL209
AILE214
AASP216
AARG218
AHOH518
AHOH584

Functional Information from PROSITE/UniProt
site_idPS00680
Number of Residues19
DetailsMAP_1 Methionine aminopeptidase subfamily 1 signature. YcGHGIHklfHtapnVp.HY
ChainResidueDetails
ATYR300-TYR318

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03174, ECO:0000269|PubMed:16724298, ECO:0000269|PubMed:16823043, ECO:0000269|PubMed:17114291
ChainResidueDetails
AHIS212
AHIS310

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03174, ECO:0000269|PubMed:16274222, ECO:0000269|PubMed:16724298, ECO:0000269|PubMed:16823043, ECO:0000269|PubMed:17114291
ChainResidueDetails
AASP229
AASP240
AHIS303
AGLU336
AGLU367

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a16
ChainResidueDetails
AASN314
AGLU336

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a16
ChainResidueDetails
AGLU336

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon