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3VP4

Crystal structure of human glutaminase in complex with inhibitor 4

Functional Information from GO Data
ChainGOidnamespacecontents
A0004359molecular_functionglutaminase activity
A0006541biological_processglutamine metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BP9 A 601
ChainResidue
AASN319
ALEU321
APHE322
ALEU323
ATYR394

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

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PDB entries from 2024-07-24

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