Structure of PDB 2vjo Chain A

Receptor sequence
>2vjoA (length=427) Species: 847 (Oxalobacter formigenes) [Search protein sequence]
TKPLDGINVLDFTHVAAGPACTQMMGFLGANVIKIERRGSGDMTRGWLQD
KPNVDSLYFTMFNCNKRSIELDMKTPEGKELLEQMIKKADVMVENFGPGA
LDRMGFTWEYIQELNPRVILASVKGYAEGHANEHLKVYENVAQCSGGAAA
TTGFWDGPPTVSGAALGDSNSGMHLMIGILAALEIRHKTGRGQKVAVAMQ
DAVLNLVRIKLRDQQRLERTGILAEYPQAQPNFAFDRDGNPLSFDNITSV
PRGGNAGGGGQPGWMLKCKGWETDADSYVYFTIAANMWPQICDMIDKPEW
KDDPAYNTFEGRVDKLMDIFSFIETKFADKDKFEVTEWAAQYGIPCGPVM
SMKELAHDPSLQKVGTVVEVVDEIRGNHLTVGAPFKFSGFQPEITRAPLL
GEHTDEVLKELGLDDAKIKELHAKQVV
3D structure
PDB2vjo Reinvestigation of the Catalytic Mechanism of Formyl-Coa Transferase, a Class III Coa-Transferase.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 A H15 A17 A18 R38 L72 M74 N96 F97 G98 R104 M105 K137 V138 Y139 D169 M200 H14 A16 A17 R37 L71 M73 N95 F96 G97 R103 M104 K136 V137 Y138 D168 M199
BS02 OXL A G258 G260 Q262 G257 G259 Q261
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:2vjo, PDBe:2vjo, PDBj:2vjo
PDBsum2vjo
PubMed18162462
UniProtO06644|FCTA_OXAFO Formyl-CoA:oxalate CoA-transferase (Gene Name=frc)

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