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1OX5

TOWARDS UNDERSTANDING THE MECHANISM OF THE COMPLEX CYCLIZATION REACTION CATALYZED BY IMIDAZOLE GLYCEROPHOSPHATE SYNTHASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0000105biological_processL-histidine biosynthetic process
A0000107molecular_functionimidazoleglycerol-phosphate synthase activity
A0004359molecular_functionglutaminase activity
A0005737cellular_componentcytoplasm
A0006541biological_processglutamine metabolic process
A0016763molecular_functionpentosyltransferase activity
A0016787molecular_functionhydrolase activity
A0016829molecular_functionlyase activity
A0016833molecular_functionoxo-acid-lyase activity
A0044281biological_processsmall molecule metabolic process
B0000105biological_processL-histidine biosynthetic process
B0000107molecular_functionimidazoleglycerol-phosphate synthase activity
B0004359molecular_functionglutaminase activity
B0005737cellular_componentcytoplasm
B0006541biological_processglutamine metabolic process
B0016763molecular_functionpentosyltransferase activity
B0016787molecular_functionhydrolase activity
B0016829molecular_functionlyase activity
B0016833molecular_functionoxo-acid-lyase activity
B0044281biological_processsmall molecule metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NI A 902
ChainResidue
AHIS-1
ASER-2
AGLY-3
AMET1
BTYR425

site_idAC2
Number of Residues25
DetailsBINDING SITE FOR RESIDUE 1PR B 891
ChainResidue
BGLY364
BTHR365
BSER402
BASP404
BGLY442
BASN469
BASP474
BGLY475
BSER499
BSER500
BGLY501
BGLY522
BALA523
BGLY524
BHOH930
BHOH931
BHOH933
BHOH934
BHOH936
BHOH958
BHOH969
BCYS243
BLYS258
BLEU297
BGLY332

site_idAC3
Number of Residues25
DetailsBINDING SITE FOR RESIDUE 1PR A 991
ChainResidue
ALEU297
AILE299
AGLY331
AGLY332
AGLY364
ATHR365
ASER402
AASP404
AGLY442
AASN469
AASP474
AGLY475
ASER499
ASER500
AGLY501
AALA523
AGLY524
AHOH1042
AHOH1043
AHOH1044
AHOH1046
AHOH1047
AHOH1067
AHOH1081
AHOH1108

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 Residues6
DetailsACT_SITE: For GATase activity => ECO:0000250
ChainResidueDetails
A5CS83
AHIS193
AGLU195
B5CS83
BHIS193
BGLU195

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000255
ChainResidueDetails
AASP245
AASP404
BASP245
BASP404

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: covalent
ChainResidueDetails
A5CS83
B5CS83

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING:
ChainResidueDetails
AGLY332
AASN469
BGLY332
BASN469

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1bxr
ChainResidueDetails
AHIS193

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1bxr
ChainResidueDetails
BHIS193

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1bxr
ChainResidueDetails
AGLU195
A5CS83
AHIS193

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1bxr
ChainResidueDetails
BGLU195
B5CS83
BHIS193

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bxr
ChainResidueDetails
AASP245
AASP404

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bxr
ChainResidueDetails
BASP245
BASP404

224004

PDB entries from 2024-08-21

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