Structure of PDB 2vjk Chain A Binding Site BS02

Receptor Information

>2vjk Chain A (length=427) Species: 847 (Oxalobacter formigenes)

TKPLDGINVLDFTHVQAGPACTQMMGFLGANVIKIERRGSGDMTRGWLQD
KPNVDSLYFTMFNCNKRSIELDMKTPEGKELLEQMIKKADVMVENFGPGA
LDRMGFTWEYIQELNPRVILASVKGYAEGHANEHLKVYENVAQCSGGAAA
TTGFWDGPPTVSGAALGDSNSGMHLMIGILAALEIRHKTGRGQKVAVAMQ
DAVLNLVRIKLRDQQRLERTGILAEYPQAQPNFAFDRDGNPLSFDNITSV
PRGGNAGGGGQPGWMLKCKGWETDADSYVYFTIAANMWPQICDMIDKPEW
KDDPAYNTFEGRVDKLMDIFSFIETKFADKDKFEVTEWAAQYGIPCGPVM
SMKELAHDPSLQKVGTVVEVVDEIRGNHLTVGAPFKFSGFQPEITRAPLL
GEHTDEVLKELGLDDAKIKELHAKQVV

Ligand information

• Ligand ID: MG
• InChI: InChI=1S/Mg/q+2
• InChIKey: JLVVSXFLKOJNIY-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Mg+2]
  CACTVS 3.341: [Mg++]
• Formula: Mg
• Name: MAGNESIUM ION
• DrugBank: DB01378
• PDB chain: 2vjk Chain A Residue 1431

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2vjk Reinvestigation of the Catalytic Mechanism of Formyl-Coa Transferase, a Class III Coa-Transferase.
• Resolution: 1.97 Å
• Binding residue (original residue number in PDB): D294 D297
• Binding residue (residue number reindexed from 1): D293 D296
• Annotation score: 1

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.

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