Structure of PDB 2vjo Chain B

Receptor sequence

>2vjoB (length=427) Species: 847 (Oxalobacter formigenes)

TKPLDGINVLDFTHVAAGPACTQMMGFLGANVIKIERRGSGDMTRGWLQD
KPNVDSLYFTMFNCNKRSIELDMKTPEGKELLEQMIKKADVMVENFGPGA
LDRMGFTWEYIQELNPRVILASVKGYAEGHANEHLKVYENVAQCSGGAAA
TTGFWDGPPTVSGAALGDSNSGMHLMIGILAALEIRHKTGRGQKVAVAMQ
DAVLNLVRIKLRDQQRLERTGILAEYPQAQPNFAFDRDGNPLSFDNITSV
PRGGNAGGGGQPGWMLKCKGWETDADSYVYFTIAANMWPQICDMIDKPEW
KDDPAYNTFEGRVDKLMDIFSFIETKFADKDKFEVTEWAAQYGIPCGPVM
SMKELAHDPSLQKVGTVVEVVDEIRGNHLTVGAPFKFSGFQPEITRAPLL
GEHTDEVLKELGLDDAKIKELHAKQVV

3D structure

• PDB: 2vjo Reinvestigation of the Catalytic Mechanism of Formyl-Coa Transferase, a Class III Coa-Transferase.
• Chain: B
• Resolution: 2.2 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): A17 E140 D169 G260 G261
• Catalytic site (residue number reindexed from 1): A16 E139 D168 G259 G260
• 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	COA	B	H15 A17 A18 R38 L72 M74 K75 N96 F97 G98 A101 R104 M105 K137 D169 M200	H14 A16 A17 R37 L71 M73 K74 N95 F96 G97 A100 R103 M104 K136 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

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:2vjo, PDBe:2vjo, PDBj:2vjo
• PDBsum: 2vjo
• PubMed: 18162462
• UniProt: O06644|FCTA_OXAFO Formyl-CoA:oxalate CoA-transferase (Gene Name=frc)