Structure of PDB 1pt5 Chain A

Receptor sequence
>1pt5A (length=415) Species: 562 (Escherichia coli) [Search protein sequence]
STPLQGIKVLDFTGVQSGPSCTQMLAWFGADVIKIERPGVGDVTRHQLRD
IPDIDALYFTMLNSNKRSIELNTKTAEGKEVMEKLIREADILVENFHPGA
IDHMGFTWEHIQEINPRLIFGSIKGFDECSPYVNVKAYENVAQAAGGAAS
TTGFWDGPPLVSAAALGDSNTGMHLLIGLLAALLHREKTGRGQRVTMSMQ
DAVLNLCRVKLRDQQRLDKLGYLEEYPQYPNGTFGDAVPRGGNAGGGGQP
GWILKCKGWETDPNAYIYFTIQEQNWENTCKAIGKPEWITDPAYSTAHAR
QPHIFDIFAEIEKYTVTIDKHEAVAYLTQFDIPCAPVLSMKEISLDPSLR
QSGSVVEVEQPLRGKYLTVGCPMKFSAFTPDIKAAPLLGEHTAAVLQELG
YSDDEIAAMKQNHAI
3D structure
PDB1pt5 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
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ACO A V16 S18 R38 L72 N73 T74 K75 N96 F97 H98 K125 K137 A138 Y139 E140 D169 M200 V15 S17 R37 L71 N72 T73 K74 N95 F96 H97 K124 K136 A137 Y138 E139 D168 M199
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

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Molecular Function
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Biological Process
External links
PDB RCSB:1pt5, PDBe:1pt5, PDBj:1pt5
PDBsum1pt5
PubMed12844490
UniProtP69902|FCTA_ECOLI Formyl-CoA:oxalate CoA-transferase (Gene Name=frc)

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