Structure of PDB 1pt8 Chain B Binding Site BS01

Receptor Information
>1pt8 Chain B (length=415) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
STPLQGIKVLDFTGVQSGPSCTQMLAWFGADVIKIERPGVGDVTRHQLRD
IPDIDALYFTMLNSNKRSIELNTKTAEGKEVMEKLIREADILVENFHPGA
IDHMGFTWEHIQEINPRLIFGSIKGFDECSPYVNVKAYENVAQAAGGAAS
TTGFWDGPPLVSAAALGDSNTGMHLLIGLLAALLHREKTGRGQRVTMSMQ
DAVLNLCRVKLRDQQRLDKLGYLEEYPQYPNGTFGDAVPRGGNAGGGGQP
GWILKCKGWETDPNAYIYFTIQEQNWENTCKAIGKPEWITDPAYSTAHAR
QPHIFDIFAEIEKYTVTIDKHEAVAYLTQFDIPCAPVLSMKEISLDPSLR
QSGSVVEVEQPLRGKYLTVGCPMKFSAFTPDIKAAPLLGEHTAAVLQELG
YSDDEIAAMKQNHAI
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 chain1pt8 Chain B Residue 752 [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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PDB1pt8 The crystal structure of the Escherichia coli yfdW gene product reveals a new fold of two interlaced rings identifying a wide family of CoA transferases.
Resolution2.2 Å
Binding residue
(original residue number in PDB)		V16 S18 R38 N73 K75 N96 F97 H98 K125 K137 A138 Y139 E140 D169 M200
Binding residue
(residue number reindexed from 1)		V15 S17 R37 N72 K74 N95 F96 H97 K124 K136 A137 Y138 E139 D168 M199
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) Q17 E140 D169 G248 G249
Catalytic site (residue number reindexed from 1) Q16 E139 D168 G247 G248
Enzyme Commision number 2.8.3.16: formyl-CoA transferase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0008410 CoA-transferase activity
GO:0016740 transferase activity
GO:0033608 formyl-CoA transferase activity
Biological Process
GO:0033611 oxalate catabolic process
GO:0071468 cellular response to acidic pH

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1pt8, PDBe:1pt8, PDBj:1pt8
PDBsum1pt8
PubMed12844490
UniProtP69902|FCTA_ECOLI Formyl-CoA:oxalate CoA-transferase (Gene Name=frc)

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