Structure of PDB 1pt8 Chain A

Receptor sequence

>1pt8A (length=416) Species: 562 (Escherichia coli)

MSTPLQGIKVLDFTGVQSGPSCTQMLAWFGADVIKIERPGVGDVTRHQLR
DIPDIDALYFTMLNSNKRSIELNTKTAEGKEVMEKLIREADILVENFHPG
AIDHMGFTWEHIQEINPRLIFGSIKGFDECSPYVNVKAYENVAQAAGGAA
STTGFWDGPPLVSAAALGDSNTGMHLLIGLLAALLHREKTGRGQRVTMSM
QDAVLNLCRVKLRDQQRLDKLGYLEEYPQYPNGTFGDAVPRGGNAGGGGQ
PGWILKCKGWETDPNAYIYFTIQEQNWENTCKAIGKPEWITDPAYSTAHA
RQPHIFDIFAEIEKYTVTIDKHEAVAYLTQFDIPCAPVLSMKEISLDPSL
RQSGSVVEVEQPLRGKYLTVGCPMKFSAFTPDIKAAPLLGEHTAAVLQEL
GYSDDEIAAMKQNHAI

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: A
• 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): Q17 E140 D169 G248 G249
• 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 Q17 S18 R38 T74 K75 N96 F97 H98 K137 A138 D169 M200	V16 Q17 S18 R38 T74 K75 N96 F97 H98 K137 A138 D169 M200
BS02	ACO	A	G248 G249	G248 G249

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)