Structure of PDB 1rqh Chain A

Receptor sequence
>1rqhA (length=471) Species: 1752 (Propionibacterium freudenreichii subsp. shermanii) [Search protein sequence]
REIEVSEPREVGITELVLRDAHQSLMATRMAMEDMVGACADIDAAGYWSV
ECWGGATYDSCIRFLNEDPWERLRTFRKLMPNSRLQMLLRGQNLLGYRHY
NDEVVDRFVDKSAENGMDVFRVFDAMNDPRNMAHAMAAVKKAGKHAQGTI
CYTISPVHTVEGYVKLAGQLLDMGADSIALKDMAALLKPQPAYDIIKAIK
DTYGQKTQINLHCHSTTGVTEVSLMKAIEAGVDVVDTAISSMSLGPGHNP
TESVAEMLEGTGYTTNLDYDRLHKIRDHFKAIRPKYKKFESKTLVDTSIF
KSQIPGGMLSNMESQLRAQGAEDKMDEVMAEVPRVRKAAGFPPLVTPSSQ
IVGTQAVFNVMMGEYKRMTGEFADIMLGYYGASPADRDPKVVKLAEEQSG
KKPITQRPADLLPPEWEKQSKEAATLKGFNGTDEDVLTYALFPQVAPVFF
EHRAEGPHSVALTDAQLKAEA
3D structure
PDB1rqh Transcarboxylase 5S structures: assembly and catalytic mechanism of a multienzyme complex subunit.
ChainA
Resolution2.0 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) D20 D124 K181 H212 H214 T346
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 D20 K181 H212 H214
BS02 PYR A Q26 G58 L91 K184 Q23 G55 L88 K181
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:1rqh, PDBe:1rqh, PDBj:1rqh
PDBsum1rqh
PubMed15329673
UniProtQ70AC7|5S_PROFR Methylmalonyl-CoA carboxyltransferase 5S subunit

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