Structure of PDB 2vjm Chain A

Receptor sequence
>2vjmA (length=427) Species: 847 (Oxalobacter formigenes) [Search protein sequence]
TKPLDGINVLDFTHVQAGPACTQMMGFLGANVIKIERRGSGDMTRGWLQD
KPNVDSLYFTMFNCNKRSIELDMKTPEGKELLEQMIKKADVMVENFGPGA
LDRMGFTWEYIQELNPRVILASVKGYAEGHANEHLKVYENVAQCSGGAAA
TTGFWDGPPTVSGAALGDSNSGMHLMIGILAALEIRHKTGRGQKVAVAMQ
DAVLNLVRIKLRDQQRLERTGILAEYPQAQPNFAFDRDGNPLSFDNITSV
PRGGNAGGGGQPGWMLKCKGWETDADSYVYFTIAANMWPQICDMIDKPEW
KDDPAYNTFEGRVDKLMDIFSFIETKFADKDKFEVTEWAAQYGIPCGPVM
SMKELAHDPSLQKVGTVVEVVDEIRGNHLTVGAPFKFSGFQPEITRAPLL
GEHTDEVLKELGLDDAKIKELHAKQVV
3D structure
PDB2vjm Reinvestigation of the Catalytic Mechanism of Formyl-Coa Transferase, a Class III Coa-Transferase.
ChainA
Resolution1.89 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 K75 N96 F97 G98 R104 M105 K137 D169 M200 H14 A17 R37 M73 K74 N95 F96 G97 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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2vjm, PDBe:2vjm, PDBj:2vjm
PDBsum2vjm
PubMed18162462
UniProtO06644|FCTA_OXAFO Formyl-CoA:oxalate CoA-transferase (Gene Name=frc)

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