Structure of PDB 1rqh Chain A Binding Site BS02

Receptor Information
>1rqh Chain A (length=471) Species: 1752 (Propionibacterium freudenreichii subsp. shermanii) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
REIEVSEPREVGITELVLRDAHQSLMATRMAMEDMVGACADIDAAGYWSV
ECWGGATYDSCIRFLNEDPWERLRTFRKLMPNSRLQMLLRGQNLLGYRHY
NDEVVDRFVDKSAENGMDVFRVFDAMNDPRNMAHAMAAVKKAGKHAQGTI
CYTISPVHTVEGYVKLAGQLLDMGADSIALKDMAALLKPQPAYDIIKAIK
DTYGQKTQINLHCHSTTGVTEVSLMKAIEAGVDVVDTAISSMSLGPGHNP
TESVAEMLEGTGYTTNLDYDRLHKIRDHFKAIRPKYKKFESKTLVDTSIF
KSQIPGGMLSNMESQLRAQGAEDKMDEVMAEVPRVRKAAGFPPLVTPSSQ
IVGTQAVFNVMMGEYKRMTGEFADIMLGYYGASPADRDPKVVKLAEEQSG
KKPITQRPADLLPPEWEKQSKEAATLKGFNGTDEDVLTYALFPQVAPVFF
EHRAEGPHSVALTDAQLKAEA
Ligand information
Ligand IDPYR
InChIInChI=1S/C3H4O3/c1-2(4)3(5)6/h1H3,(H,5,6)
InChIKeyLCTONWCANYUPML-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.385CC(=O)C(O)=O
OpenEye OEToolkits 1.7.6CC(=O)C(=O)O
ACDLabs 12.01O=C(C(=O)O)C
FormulaC3 H4 O3
NamePYRUVIC ACID
ChEMBLCHEMBL1162144
DrugBankDB00119
ZINCZINC000001532517
PDB chain1rqh Chain A Residue 602 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1rqh Transcarboxylase 5S structures: assembly and catalytic mechanism of a multienzyme complex subunit.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		Q26 G58 L91 K184
Binding residue
(residue number reindexed from 1)		Q23 G55 L88 K181
Annotation score5
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.
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

[Back to BioLiP]