Structure of PDB 2vjk Chain B

Receptor sequence
>2vjkB (length=427) Species: 847 (Oxalobacter formigenes) [Search protein sequence]
TKPLDGINVLDFTHVQAGPACTQMMGFLGANVIKIERRGSGDMTRGWLQD
KPNVDSLYFTMFNCNKRSIELDMKTPEGKELLEQMIKKADVMVENFGPGA
LDRMGFTWEYIQELNPRVILASVKGYAEGHANEHLKVYENVAQCSGGAAA
TTGFWDGPPTVSGAALGDSNSGMHLMIGILAALEIRHKTGRGQKVAVAMQ
DAVLNLVRIKLRDQQRLERTGILAEYPQAQPNFAFDRDGNPLSFDNITSV
PRGGNAGGGGQPGWMLKCKGWETDADSYVYFTIAANMWPQICDMIDKPEW
KDDPAYNTFEGRVDKLMDIFSFIETKFADKDKFEVTEWAAQYGIPCGPVM
SMKELAHDPSLQKVGTVVEVVDEIRGNHLTVGAPFKFSGFQPEITRAPLL
GEHTDEVLKELGLDDAKIKELHAKQVV
3D structure
PDB2vjk Reinvestigation of the Catalytic Mechanism of Formyl-Coa Transferase, a Class III Coa-Transferase.
ChainB
Resolution1.97 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 B H15 V16 Q17 R38 M44 L72 M74 F97 R104 M105 Y139 E140 D169 H14 V15 Q16 R37 M43 L71 M73 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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2vjk, PDBe:2vjk, PDBj:2vjk
PDBsum2vjk
PubMed18162462
UniProtO06644|FCTA_OXAFO Formyl-CoA:oxalate CoA-transferase (Gene Name=frc)

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