Structure of PDB 6aby Chain B Binding Site BS02

Receptor Information
>6aby Chain B (length=371) Species: 399549 (Metallosphaera sedula DSM 5348) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MELRKGLEDIAIKETSITYIDGELGRLYYRGYSIFDLASFSNFEEVAYLL
WYGKLPTRHELDDFKSRLAEERSISEDISTFVKRTAKFGNPMDILRTTVS
MMGLEDRSEGDLIGKAIKMTAKIPTIISLIQRTRRNQEFVEPDPSLSHSE
NFLYMIRGERPSPSDTRVLDVSLMLHMDHEMNASTMACLVVASTLSDIYS
SVVAGISALKGPLHGGANSEALKQFMEIETPDNVEKYVMNKLSSGQRLMG
FGHRIYKTMDPRAKILKEYANQLSKNEEIKRLFEIANRVEEIGIKILGKR
GIYPNVDFYSGLVFYAMGFDPDLFPTIFASARVIGWTAHVDEYLKDNKLI
RPKAIYVGDLGKRYVPIEERL
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 chain6aby Chain B Residue 403 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6aby Structural insights into the inhibition properties of archaeon citrate synthase from Metallosphaera sedula.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		R247 L248 F251 R300 I302
Binding residue
(residue number reindexed from 1)		R247 L248 F251 R300 I302
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) S184 H214 H253 R262 D307
Catalytic site (residue number reindexed from 1) S184 H214 H253 R262 D307
Enzyme Commision number 2.3.3.16: citrate synthase (unknown stereospecificity).
Gene Ontology
Molecular Function
GO:0004108 citrate (Si)-synthase activity
GO:0016746 acyltransferase activity
GO:0036440 citrate synthase activity
GO:0046912 acyltransferase activity, acyl groups converted into alkyl on transfer
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006099 tricarboxylic acid cycle
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6aby, PDBe:6aby, PDBj:6aby
PDBsum6aby
PubMed30794680
UniProtA4YGX6

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