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3ZR4

STRUCTURAL EVIDENCE FOR AMMONIA TUNNELING ACROSS THE (BETA-ALPHA)8 BARREL OF THE IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE BIENZYME COMPLEX

Functional Information from GO Data
ChainGOidnamespacecontents
A0000105biological_processL-histidine biosynthetic process
A0000107molecular_functionimidazoleglycerol-phosphate synthase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0016829molecular_functionlyase activity
B0000105biological_processL-histidine biosynthetic process
B0000107molecular_functionimidazoleglycerol-phosphate synthase activity
B0004359molecular_functionglutaminase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0006541biological_processglutamine metabolic process
B0016763molecular_functionpentosyltransferase activity
B0016787molecular_functionhydrolase activity
B0016829molecular_functionlyase activity
C0000105biological_processL-histidine biosynthetic process
C0000107molecular_functionimidazoleglycerol-phosphate synthase activity
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0016829molecular_functionlyase activity
D0000105biological_processL-histidine biosynthetic process
D0000107molecular_functionimidazoleglycerol-phosphate synthase activity
D0004359molecular_functionglutaminase activity
D0005515molecular_functionprotein binding
D0005737cellular_componentcytoplasm
D0006541biological_processglutamine metabolic process
D0016763molecular_functionpentosyltransferase activity
D0016787molecular_functionhydrolase activity
D0016829molecular_functionlyase activity
E0000105biological_processL-histidine biosynthetic process
E0000107molecular_functionimidazoleglycerol-phosphate synthase activity
E0005515molecular_functionprotein binding
E0005737cellular_componentcytoplasm
E0016829molecular_functionlyase activity
F0000105biological_processL-histidine biosynthetic process
F0000107molecular_functionimidazoleglycerol-phosphate synthase activity
F0004359molecular_functionglutaminase activity
F0005515molecular_functionprotein binding
F0005737cellular_componentcytoplasm
F0006541biological_processglutamine metabolic process
F0016763molecular_functionpentosyltransferase activity
F0016787molecular_functionhydrolase activity
F0016829molecular_functionlyase activity
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GOL A 1202
ChainResidue
AGLU231

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 1201
ChainResidue
BPRO38
BARG39
BASN40

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GLN B 1205
ChainResidue
BGLU96
BVAL140
BHIS141
BTHR142
BTYR143
BHOH2030
BHOH2036
AGLN123
BVAL51
BGLY52
BCYS84
BGLN88

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GOL B 1202
ChainResidue
BLYS72

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL C 1254
ChainResidue
CASN148
CTHR149
CGLY150
CHOH2035
DASN26

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL D 1201
ChainResidue
DLYS129
DASP130

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GLN D 1205
ChainResidue
DGLY52
DGLN88
DGLU96
DVAL140
DHIS141
DTHR142
DTYR143
DHOH2029

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL E 1254
ChainResidue
EARG188
ELEU215

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL E 1255
ChainResidue
DGLU36
EARG188
EPHE189

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Nucleophile
ChainResidueDetails
BCYS84
DCYS84
FCYS84
CASP130
EASP11
EASP130

site_idSWS_FT_FI2
Number of Residues6
DetailsACT_SITE:
ChainResidueDetails
BHIS178
BGLU180
DHIS178
DGLU180
FHIS178
FGLU180

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 2024-07-17

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