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2WJZ

Crystal structure of (HisH) K181A Y138A mutant of imidazoleglycerolphosphate synthase (HisH HisF) which displays constitutive glutaminase activity

Functional Information from GO Data
ChainGOidnamespacecontents
A0000105biological_processL-histidine biosynthetic process
A0000107molecular_functionimidazoleglycerol-phosphate synthase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
B0000105biological_processL-histidine biosynthetic process
B0000107molecular_functionimidazoleglycerol-phosphate synthase activity
B0004359molecular_functionglutaminase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0009382cellular_componentimidazoleglycerol-phosphate synthase complex
B0016763molecular_functionpentosyltransferase activity
C0000105biological_processL-histidine biosynthetic process
C0000107molecular_functionimidazoleglycerol-phosphate synthase activity
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
D0000105biological_processL-histidine biosynthetic process
D0000107molecular_functionimidazoleglycerol-phosphate synthase activity
D0004359molecular_functionglutaminase activity
D0005515molecular_functionprotein binding
D0005737cellular_componentcytoplasm
D0009382cellular_componentimidazoleglycerol-phosphate synthase complex
D0016763molecular_functionpentosyltransferase activity
E0000105biological_processL-histidine biosynthetic process
E0000107molecular_functionimidazoleglycerol-phosphate synthase activity
E0005515molecular_functionprotein binding
E0005737cellular_componentcytoplasm
F0000105biological_processL-histidine biosynthetic process
F0000107molecular_functionimidazoleglycerol-phosphate synthase activity
F0004359molecular_functionglutaminase activity
F0005515molecular_functionprotein binding
F0005737cellular_componentcytoplasm
F0009382cellular_componentimidazoleglycerol-phosphate synthase complex
F0016763molecular_functionpentosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 1252
ChainResidue
AGLY81
AGLY82
AASN103
ATHR104
AHOH2043

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 C 1252
ChainResidue
CHOH2059
CGLY82
CASN103
CTHR104
CHOH2015

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 E 1252
ChainResidue
EGLY82
EASN103
ETHR104

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsActive site: {"description":"Nucleophile"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsActive site: {}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 753
ChainResidueDetails
AASP11proton acceptor, proton donor
AASP130proton acceptor, proton donor

site_idMCSA2
Number of Residues2
DetailsM-CSA 753
ChainResidueDetails
CASP11proton acceptor, proton donor
CASP130proton acceptor, proton donor

site_idMCSA3
Number of Residues2
DetailsM-CSA 753
ChainResidueDetails
EASP11proton acceptor, proton donor
EASP130proton acceptor, proton donor

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PDB entries from 2026-05-13

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