Structure of PDB 2vjl Chain B

Receptor sequence

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

TKPLDGINVLDFTHVQAGPACTQMMGFLGANVIKIERRGSGDMTRGWLQD
KPNVDSLYFTMFNCNKRSIELDMKTPEGKELLEQMIKKADVMVENFGPGA
LDRMGFTWEYIQELNPRVILASVKGYAEGHANEHLKVYENVAQCSGGAAA
TTGFWDGPPTVSGAALGDSNSGMHLMIGILAALEIRHKTGRGQKVAVAMQ
DAVLNLVRIKLRDQQRLERTGILAEYPQAQPNFAFDRDGNPLSFDNITSV
PRGGNAGGGGQPGWMLKCKGWETDADSYVYFTIAANMWPQICDMIDKPEW
KDDPAYNTFEGRVDKLMDIFSFIETKFADKDKFEVTEWAAQYGIPCGPVM
SMKELAHDPSLQKVGTVVEVVDEIRGNHLTVGAPFKFSGFQPEITRAPLL
GEHTDEVLKELGLDDAKIKELHAKQVV

3D structure

• PDB: 2vjl Reinvestigation of the Catalytic Mechanism of Formyl-Coa Transferase, a Class III Coa-Transferase.
• Chain: B
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Q17 E140 D169 G260 G261
• Catalytic site (residue number reindexed from 1): Q16 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 V16 Q17 R38 M44 L72 M74 K75 F97 R104 M105 Y139 E140 D169	H14 V15 Q16 R37 M43 L71 M73 K74 F96 R103 M104 Y138 E139 D168

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