Structure of PDB 1pt8 Chain B

Receptor sequence

>1pt8B (length=415) Species: 562 (Escherichia coli)

STPLQGIKVLDFTGVQSGPSCTQMLAWFGADVIKIERPGVGDVTRHQLRD
IPDIDALYFTMLNSNKRSIELNTKTAEGKEVMEKLIREADILVENFHPGA
IDHMGFTWEHIQEINPRLIFGSIKGFDECSPYVNVKAYENVAQAAGGAAS
TTGFWDGPPLVSAAALGDSNTGMHLLIGLLAALLHREKTGRGQRVTMSMQ
DAVLNLCRVKLRDQQRLDKLGYLEEYPQYPNGTFGDAVPRGGNAGGGGQP
GWILKCKGWETDPNAYIYFTIQEQNWENTCKAIGKPEWITDPAYSTAHAR
QPHIFDIFAEIEKYTVTIDKHEAVAYLTQFDIPCAPVLSMKEISLDPSLR
QSGSVVEVEQPLRGKYLTVGCPMKFSAFTPDIKAAPLLGEHTAAVLQELG
YSDDEIAAMKQNHAI

3D structure

• PDB: 1pt8 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.
• Chain: B
• Resolution: 2.2 Å

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	B	V16 S18 R38 N73 K75 N96 F97 H98 K125 K137 A138 Y139 E140 D169 M200	V15 S17 R37 N72 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

External links

• PDB: RCSB:1pt8, PDBe:1pt8, PDBj:1pt8
• PDBsum: 1pt8
• PubMed: 12844490
• UniProt: P69902|FCTA_ECOLI Formyl-CoA:oxalate CoA-transferase (Gene Name=frc)