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

3SS4

Crystal structure of mouse Glutaminase C, phosphate-bound form

Functional Information from GO Data
ChainGOidnamespacecontents
A0004359molecular_functionglutaminase activity
A0006541biological_processglutamine metabolic process
B0004359molecular_functionglutaminase activity
B0006541biological_processglutamine metabolic process
C0004359molecular_functionglutaminase activity
C0006541biological_processglutamine metabolic process
D0004359molecular_functionglutaminase activity
D0006541biological_processglutamine metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 1
ChainResidue
AHOH29
ASER291
AASN340
ATYR471
AHOH611

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 B 2
ChainResidue
BHOH614
BHOH94
BSER291
BASN340
BTYR471

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 C 3
ChainResidue
CSER291
CASN340
CTYR471
CHOH613

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 D 4
ChainResidue
DSER291
DASN340
DARG392
DHOH629

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues28
DetailsBINDING: BINDING => ECO:0000269|PubMed:22228304, ECO:0007744|PDB:3SS5
ChainResidueDetails
AVAL285
BASN380
BARG387
BVAL413
BMET465
BLEU483
CVAL285
CPRO334
CASN380
CARG387
CVAL413
APRO334
CMET465
CLEU483
DVAL285
DPRO334
DASN380
DARG387
DVAL413
DMET465
DLEU483
AASN380
AARG387
AVAL413
AMET465
ALEU483
BVAL285
BPRO334

site_idSWS_FT_FI2
Number of Residues8
DetailsMOD_RES: N6-succinyllysine => ECO:0007744|PubMed:23806337
ChainResidueDetails
AVAL129
ALYS163
BVAL129
BLYS163
CVAL129
CLYS163
DVAL129
DLYS163

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:O94925
ChainResidueDetails
AVAL310
BVAL310
CVAL310
DVAL310

225158

건을2024-09-18부터공개중

PDB statisticsPDBj update infoContact PDBjnumon