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3VP1

Crystal structure of human glutaminase in complex with L-glutamate and BPTES

Functional Information from GO Data
ChainGOidnamespacecontents
A0004359molecular_functionglutaminase activity
A0006541biological_processglutamine metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 04A A 601
ChainResidue
AARG317
AARG317
APHE318
ALYS320
APHE322
APHE322
ALEU323
AASN324
ATYR394

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GLU A 602
ChainResidue
ATYR249
AGLN285
ASER286
AASN335
AGLU381
AASN388
ATYR414
ATYR466
AVAL484

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 603
ChainResidue
APHE373
ASER374
AASN375
AASN375
AALA376
AALA376
AHOH726
AHOH726
AHOH762
AHOH762

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 604
ChainResidue
ALYS320
AARG387
ATYR394
ALYS398

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:22049910, ECO:0000269|PubMed:22538822, ECO:0000305|PubMed:24451979, ECO:0007744|PDB:3CZD, ECO:0007744|PDB:3UNW, ECO:0007744|PDB:3VP0, ECO:0007744|PDB:3VP1
ChainResidueDetails
ASER286
AASN335
AGLU381
ATYR414
ATYR466
AVAL484

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:22049910, ECO:0000269|PubMed:22538822, ECO:0000305|PubMed:24451979, ECO:0007744|PDB:3CZD, ECO:0007744|PDB:3UNW, ECO:0007744|PDB:3VP1
ChainResidueDetails
AASN388

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS311

227111

PDB entries from 2024-11-06

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