Structure of PDB 2vjl Chain A

Receptor sequence

>2vjlA (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: A
• 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	A	H15 A18 R38 M74 N96 F97 G98 R104 M105 K137 Y139 D169 M200	H14 A17 R37 M73 N95 F96 G97 R103 M104 K136 Y138 D168 M199
BS02	MG	A	D294 D297	D293 D296
BS03	MG	A	G222 F245 I248	G221 F244 I247

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)