Structure of PDB 1rqb Chain A

Receptor sequence
>1rqbA (length=472) Species: 1752 (Propionibacterium freudenreichii subsp. shermanii) [Search protein sequence]
PREIEVSEPREVGITELVLRDAHQSLMATRMAMEDMVGACADIDAAGYWS
VECWGGATYDSCIRFLNEDPWERLRTFRKLMPNSRLQMLLRGQNLLGYRH
YNDEVVDRFVDKSAENGMDVFRVFDAMNDPRNMAHAMAAVKKAGKHAQGT
ICYTISPVHTVEGYVKLAGQLLDMGADSIALKDMAALLKPQPAYDIIKAI
KDTYGQKTQINLHCHSTTGVTEVSLMKAIEAGVDVVDTAISSMSLGPGHN
PTESVAEMLEGTGYTTNLDYDRLHKIRDHFKAIRPKYKKFESKTLVDTSI
FKSQIPGGMLSNMESQLRAQGAEDKMDEVMAEVPRVRKAAGFPPLVTPSS
QIVGTQAVFNVMMGEYKRMTGEFADIMLGYYGASPADRDPKVVKLAEEQS
GKKPITQRPADLLPPEWEKQSKEAATLKGFNGTDEDVLTYALFPQVAPVF
FEHRAEGPHSVALTDAQLKAEA
3D structure
PDB1rqb Transcarboxylase 5S structures: assembly and catalytic mechanism of a multienzyme complex subunit.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D23 D127 K184 H215 H217 T349
Catalytic site (residue number reindexed from 1) D21 D125 K182 H213 H215 T347
Enzyme Commision number 2.1.3.1: methylmalonyl-CoA carboxytransferase.
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 CO A D23 K184 H215 H217 D21 K182 H213 H215
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016740 transferase activity
GO:0046872 metal ion binding
GO:0047154 methylmalonyl-CoA carboxytransferase activity

View graph for
Molecular Function
External links
PDB RCSB:1rqb, PDBe:1rqb, PDBj:1rqb
PDBsum1rqb
PubMed15329673
UniProtQ70AC7|5S_PROFR Methylmalonyl-CoA carboxyltransferase 5S subunit

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