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1JVN

CRYSTAL STRUCTURE OF IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE: A TUNNEL THROUGH A (BETA/ALPHA)8 BARREL JOINS TWO ACTIVE SITES

Functional Information from GO Data
ChainGOidnamespacecontents
A0000105biological_processL-histidine biosynthetic process
A0000107molecular_functionimidazoleglycerol-phosphate synthase activity
A0004359molecular_functionglutaminase activity
A0005737cellular_componentcytoplasm
A0016763molecular_functionpentosyltransferase activity
B0000105biological_processL-histidine biosynthetic process
B0000107molecular_functionimidazoleglycerol-phosphate synthase activity
B0004359molecular_functionglutaminase activity
B0005737cellular_componentcytoplasm
B0016763molecular_functionpentosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NI B 901
ChainResidue
BHIS-1
BSER-2
BGLY-3
BMET1

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NI A 902
ChainResidue
AHIS-1
AGLY-3
ASER-2
AMET1
BTYR425

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 801
ChainResidue
AGLY331
AGLY364
ATHR365
AHOH1010

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 802
ChainResidue
AGLY475
AASN477
AGLY524
AARG528
AHOH974
AHOH1073
AHOH1103

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 803
ChainResidue
BLYS158
BLYS170
BLYS343
BHOH1136

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 804
ChainResidue
BGLY331
BGLY364
BTHR365
BHOH1012
BHOH1132
BHOH1172

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 806
ChainResidue
ASER130
AGLU131
AASN132
BLYS493

site_idAC8
Number of Residues10
DetailsBINDING SITE FOR RESIDUE POP B 999
ChainResidue
BASP474
BGLY475
BASN477
BGLY501
BGLY524
BMET525
BARG528
BHOH1013
BHOH1052
BHOH1113

Functional Information from PROSITE/UniProt
site_idPS00599
Number of Residues10
DetailsAA_TRANSFER_CLASS_2 Aminotransferases class-II pyridoxal-phosphate attachment site. TISKAYGAQA
ChainResidueDetails
ATHR389-ALA398

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsRegion: {"description":"PRFAR binding"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsActive site: {"description":"For GATase activity","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"description":"covalent"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsBinding site: {}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1bxr
ChainResidueDetails
AGLU195
A14383
AHIS193

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1bxr
ChainResidueDetails
BGLU195
B14383
BHIS193

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bxr
ChainResidueDetails
AASP245
AASP404

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bxr
ChainResidueDetails
BASP245
BASP404

site_idCSA5
Number of Residues1
DetailsAnnotated By Reference To The Literature 1bxr
ChainResidueDetails
AHIS193

site_idCSA6
Number of Residues1
DetailsAnnotated By Reference To The Literature 1bxr
ChainResidueDetails
BHIS193

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PDB entries from 2026-04-08

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