Structure of PDB 1ox5 Chain A Binding Site BS01

Receptor Information
>1ox5 Chain A (length=532) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GSHMPVVHVIDVESGNLQSLTNAIEHLGYEVQLVKSPKDFNISGTSRLIL
PGVGNYGHFVDNLFNRGFEKPIREYIESGKPIMGICVGLQALFAGSVESP
KSTGLNYIDFKLSRFDDSEKPVPEIGWNSCIPSENLFFGLDPYKRYYFVH
SFAAILNSEKKKNLENDGWKIAKAKYGSEEFIAAVNKNNIFATQFHPEKS
GKAGLNVIENFLKQQSPPIPNYSAEEKELLMNDYSNYGLTRRIIACLDVR
TNDQGDLVVTKLGKPVQLAQKYYQQGADEVTFLNITCPLKDTPMLEVLKQ
AAKTVFVPLTVGGGIKDIVDVDGTKIPALEVASLYFRSGADKVSIGTDAV
YAAEKYYELGNRGDGTSPIETISKAYGAQAVVISVDPKRVYVNSQADTKN
KVFETEYPGPNGEKYCWYQCTIKGGRESRDLGVWELTRACEALGAGEILL
NCIDKDGSNSGYDLELIEHVKDAVKIPVIASSGAGVPEHFEEAFLKTRAD
ACLGAGMFHRGEFTVNDVKEYLLEHGLKVRMD
Ligand information
Ligand ID1PR
InChIInChI=1S/C15H29N5O15P2/c16-13(26)9-14(18-4-17-1-6(21)10(23)7(22)2-33-36(27,28)29)20(5-19-9)15-12(25)11(24)8(35-15)3-34-37(30,31)32/h5-8,10-12,15,17-18,21-25H,1-4H2,(H2,16,26)(H2,27,28,29)(H2,30,31,32)/t6?,7-,8-,10+,11-,12-,15-/m1/s1
InChIKeyHDCXLRQQJHBDSI-DYHIIFNWSA-N
SMILES
SoftwareSMILES
CACTVS 3.341NC(=O)c1ncn([CH]2O[CH](CO[P](O)(O)=O)[CH](O)[CH]2O)c1NCNC[CH](O)[CH](O)[CH](O)CO[P](O)(O)=O
OpenEye OEToolkits 1.5.0c1nc(c(n1C2C(C(C(O2)COP(=O)(O)O)O)O)NCNCC(C(C(COP(=O)(O)O)O)O)O)C(=O)N
OpenEye OEToolkits 1.5.0c1nc(c(n1[C@H]2[C@@H]([C@@H]([C@H](O2)COP(=O)(O)O)O)O)NCNCC([C@@H]([C@@H](COP(=O)(O)O)O)O)O)C(=O)N
CACTVS 3.341NC(=O)c1ncn([C@@H]2O[C@H](CO[P](O)(O)=O)[C@@H](O)[C@H]2O)c1NCNC[C@@H](O)[C@H](O)[C@H](O)CO[P](O)(O)=O
FormulaC15 H29 N5 O15 P2
NamePHOSPHORIC ACID MONO-[5-({[5-CARBAMOYL-3-(5-PHOSPHONOOXY-5-DEOXY-RIBOFURANOSYL)- 3H-IMIDAZOL-4-YLAMINO]-METHYL}-AMINO)-2,3,4-TRIHYDROXY-PENTYL] ESTER
ChEMBL
DrugBank
ZINC
PDB chain1ox5 Chain A Residue 991 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1ox5 Towards Understanding the Mechanism of the Complex Cyclization Reaction Catalyzed by Imidazole Glycerophosphate Synthase:Crystal Structures of a Ternary Complex and the Free Enzyme
Resolution2.5 Å
Binding residue
(original residue number in PDB)		L297 I299 G331 G364 T365 S402 D404 G442 N469 D474 G475 S500 A523 G524
Binding residue
(residue number reindexed from 1)		L283 I285 G313 G346 T347 S384 D386 G424 N451 D456 G457 S482 A505 G506
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) D245 D404
Catalytic site (residue number reindexed from 1) D248 D386
Enzyme Commision number 3.5.1.2: glutaminase.
4.3.2.10: imidazole glycerol-phosphate synthase.
Gene Ontology
Molecular Function
GO:0000107 imidazoleglycerol-phosphate synthase activity
GO:0004359 glutaminase activity
GO:0016763 pentosyltransferase activity
GO:0016787 hydrolase activity
GO:0016829 lyase activity
GO:0016833 oxo-acid-lyase activity
Biological Process
GO:0000105 L-histidine biosynthetic process
GO:0006541 glutamine metabolic process
GO:0044281 small molecule metabolic process
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function
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Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1ox5, PDBe:1ox5, PDBj:1ox5
PDBsum1ox5
PubMed12795595
UniProtP33734|HIS5_YEAST Imidazole glycerol phosphate synthase hisHF (Gene Name=HIS7)

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