Structure of PDB 3bli Chain A Binding Site BS02

Receptor Information
>3bli Chain A (length=311) Species: 173 (Leptospira interrogans) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
RLEILDVTLRDGEQTRGVSFSTSEKLNIAKFLLQKLNVDRVEIASARVSK
GELETVQKIMEWAATEQLTERIEILGFVDGNKTVDWIKDSGAKVLNLLTK
GSLHHLEKQLGKTPKEFFTDVSFVIEYAIKSGLKINVYLEDWSNGFRNSP
DYVKSLVEHLSKEHIERIFLPDTLGVLSPEETFQGVDSLIQKYPDIHFEF
HGHNDYDLSVANSLQAIRAGVKGLHASINGLGERAGNTPLEALVTTIHDK
SNSKTNINEIAITEASRLVEVFSGKRISANRPIVGEDVFTQTAGVNLYAN
PILPERFGRKR
Ligand information
Ligand IDACO
InChIInChI=1S/C23H38N7O17P3S/c1-12(31)51-7-6-25-14(32)4-5-26-21(35)18(34)23(2,3)9-44-50(41,42)47-49(39,40)43-8-13-17(46-48(36,37)38)16(33)22(45-13)30-11-29-15-19(24)27-10-28-20(15)30/h10-11,13,16-18,22,33-34H,4-9H2,1-3H3,(H,25,32)(H,26,35)(H,39,40)(H,41,42)(H2,24,27,28)(H2,36,37,38)/t13-,16-,17-,18+,22-/m1/s1
InChIKeyZSLZBFCDCINBPY-ZSJPKINUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)CO[P@](=O)(O)O[P@@](=O)(O)OC[C@@H]1[C@H]([C@H]([C@@H](O1)n2cnc3c2ncnc3N)O)OP(=O)(O)O)O
CACTVS 3.341CC(=O)SCCNC(=O)CCNC(=O)[C@H](O)C(C)(C)CO[P@@](O)(=O)O[P@](O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1O[P](O)(O)=O)n2cnc3c(N)ncnc23
ACDLabs 10.04O=C(SCCNC(=O)CCNC(=O)C(O)C(C)(C)COP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3OP(=O)(O)O)C
CACTVS 3.341CC(=O)SCCNC(=O)CCNC(=O)[CH](O)C(C)(C)CO[P](O)(=O)O[P](O)(=O)OC[CH]1O[CH]([CH](O)[CH]1O[P](O)(O)=O)n2cnc3c(N)ncnc23
OpenEye OEToolkits 1.5.0CC(=O)SCCNC(=O)CCNC(=O)C(C(C)(C)COP(=O)(O)OP(=O)(O)OCC1C(C(C(O1)n2cnc3c2ncnc3N)O)OP(=O)(O)O)O
FormulaC23 H38 N7 O17 P3 S
NameACETYL COENZYME *A
ChEMBLCHEMBL1230809
DrugBank
ZINCZINC000008551095
PDB chain3bli Chain A Residue 1004 [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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PDB3bli Molecular basis of the substrate specificity and the catalytic mechanism of citramalate synthase from Leptospira interrogans
Resolution2.5 Å
Binding residue
(original residue number in PDB)		Q20 R53 V54 E146
Binding residue
(residue number reindexed from 1)		Q14 R47 V48 E140
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) Q20
Catalytic site (residue number reindexed from 1) Q14
Enzyme Commision number 2.3.3.21: (R)-citramalate synthase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0046912 acyltransferase activity, acyl groups converted into alkyl on transfer
Biological Process
GO:0019752 carboxylic acid metabolic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3bli, PDBe:3bli, PDBj:3bli
PDBsum3bli
PubMed18498255
UniProtQ8F3Q1|CIMA_LEPIN (R)-citramalate synthase CimA (Gene Name=cimA)

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