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4BQM

Crystal structure of human liver-type glutaminase, catalytic domain

Functional Information from GO Data
ChainGOidnamespacecontents
A0004359molecular_functionglutaminase activity
A0006541biological_processglutamine metabolic process
B0004359molecular_functionglutaminase activity
B0006541biological_processglutamine metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 1466
ChainResidue
APHE334
APRO335
ALYS336
AHOH2026
BHIS163
BLEU457
BPHE458

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 1467
ChainResidue
AASN264
AVAL267
ASER395
APRO246
ASER247

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 1468
ChainResidue
AASP236
AHIS239
ALYS240
AHOH2034

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 1466
ChainResidue
ASER395
BHIS394
BSER395
BALA406

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 1467
ChainResidue
BPRO246
BSER247
BASN264
BVAL267
BCYS396
BTYR399
BHOH2062

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 1468
ChainResidue
BTYR322
BASP345

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 1469
ChainResidue
AASP345

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:O94925
ChainResidueDetails
ASER219
BGLU314
BASN321
BTYR347
BTYR399
BVAL417
AASN268
AGLU314
AASN321
ATYR347
ATYR399
AVAL417
BSER219
BASN268

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q571F8
ChainResidueDetails
ALYS253
BLYS253

site_idSWS_FT_FI3
Number of Residues6
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q571F8
ChainResidueDetails
ALYS279
ALYS284
ALYS329
BLYS279
BLYS284
BLYS329

224004

PDB entries from 2024-08-21

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