Structure of PDB 1a59 Chain A Binding Site BS01

Receptor Information
>1a59 Chain A (length=377) Species: 56673 (Antarctic bacterium DS2-3R) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EPTIHKGLAGVTADVTAISKVNSDTNSLLYRGYPVQELAAKCSFEQVAYL
LWNSELPNDSELKAFVNFERSHRKLDENVKGAIDLLSTACHPMDVARTAV
SVLGANHARAQDSSPEANLEKAMSLLATFPSVVAYDQRRRRGEELIEPRE
DLDYSANFLWMTFGEEAAPEVVEAFNVSMILYAEHSFNASTFTARVITST
LADLHSAVTGAIGALKGPLHGGANEAVMHTFEEIGIRKDESLDEAATRSK
AWMVDALAQKKKVMGFGHRVYKNGDSRVPTMKSALDAMIKHYDRPEMLGL
YNGLEAAMEEAKQIKPNLDYPAGPTYNLMGFDTEMFTPLFIAARITGWTA
HIMEQVADNALIRPLSEYNGPEQRQVP
Ligand information
Ligand IDCOA
InChIInChI=1S/C21H36N7O16P3S/c1-21(2,16(31)19(32)24-4-3-12(29)23-5-6-48)8-41-47(38,39)44-46(36,37)40-7-11-15(43-45(33,34)35)14(30)20(42-11)28-10-27-13-17(22)25-9-26-18(13)28/h9-11,14-16,20,30-31,48H,3-8H2,1-2H3,(H,23,29)(H,24,32)(H,36,37)(H,38,39)(H2,22,25,26)(H2,33,34,35)/t11-,14-,15-,16+,20-/m1/s1
InChIKeyRGJOEKWQDUBAIZ-IBOSZNHHSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CC(C)(COP(=O)(O)OP(=O)(O)OCC1C(C(C(O1)n2cnc3c2ncnc3N)O)OP(=O)(O)O)C(C(=O)NCCC(=O)NCCS)O
CACTVS 3.341CC(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)[C@@H](O)C(=O)NCCC(=O)NCCS
OpenEye OEToolkits 1.5.0CC(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)[C@H](C(=O)NCCC(=O)NCCS)O
CACTVS 3.341CC(C)(CO[P](O)(=O)O[P](O)(=O)OC[CH]1O[CH]([CH](O)[CH]1O[P](O)(O)=O)n2cnc3c(N)ncnc23)[CH](O)C(=O)NCCC(=O)NCCS
ACDLabs 10.04O=C(NCCS)CCNC(=O)C(O)C(C)(C)COP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3OP(=O)(O)O
FormulaC21 H36 N7 O16 P3 S
NameCOENZYME A
ChEMBLCHEMBL1213327
DrugBankDB01992
ZINCZINC000008551087
PDB chain1a59 Chain A Residue 380 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1a59 Structural adaptations of the cold-active citrate synthase from an Antarctic bacterium.
Resolution2.09 Å
Binding residue
(original residue number in PDB)		L220 A224 K263 V264 M265 G266 F267 G268 H269 R270 I315 N318
Binding residue
(residue number reindexed from 1)		L219 A223 K262 V263 M264 G265 F266 G267 H268 R269 I314 N317
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) S191 H221 H269 R278 D320
Catalytic site (residue number reindexed from 1) S190 H220 H268 R277 D319
Enzyme Commision number 2.3.3.16: citrate synthase (unknown stereospecificity).
2.3.3.5: 2-methylcitrate synthase.
Gene Ontology
Molecular Function
GO:0004108 citrate (Si)-synthase activity
GO:0016740 transferase activity
GO:0036440 citrate synthase activity
GO:0046912 acyltransferase activity, acyl groups converted into alkyl on transfer
GO:0050440 2-methylcitrate synthase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006099 tricarboxylic acid cycle
GO:0019679 propionate metabolic process, methylcitrate 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:1a59, PDBe:1a59, PDBj:1a59
PDBsum1a59
PubMed9551556
UniProtO34002|PRPC_ABDS2 2-methylcitrate synthase (Gene Name=gltA)

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