› 1dd2

Solution NMR

BIOTIN CARBOXYL CARRIER DOMAIN OF TRANSCARBOXYLASE (TC 1.3S)

Released:
DOI: 10.2210/pdb1dd2/pdb
PDB entry 1dd2 coloured by chain, ensemble of 32 models, front view.
PDB entry 1dd2 coloured by chain, ensemble of 32 models, side view.
PDB entry 1dd2 coloured by chain, ensemble of 32 models, top view.
Source organism: Propionibacterium freudenreichii subsp. shermanii
Primary publication:
High resolution solution structure of the 1.3S subunit of transcarboxylase from Propionibacterium shermanii.
Reddy DV, Shenoy BC, Carey PR, Sönnichsen FD
Biochemistry 39 2509-16 (2000)
PMID: 10704200

Function and Biology Details

Reaction catalysed: 
(S)-methylmalonyl-CoA + pyruvate = propanoyl-CoA + oxaloacetate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136368 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methylmalonyl-CoA carboxyltransferase 1.3S subunit Chain: A
Molecule details ›
Chain: A
Length: 77 amino acids
Theoretical weight: 7.82 KDa
Source organism: Propionibacterium freudenreichii subsp. shermanii
Expression system: Escherichia coli
UniProt:
  • Canonical: P02904 (Residues: 47-123; Coverage: 63%)
Sequence domains: Biotin-requiring enzyme
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: DISTANCE GEOMETRY/SIMULATED ANNEALING HYBRID METHOD
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Multi-subunit acetyl-CoA carboxylases.
Cronan et al. (2002)
7 more

1 mention without citation

Crystal structure of the carboxyltransferase subunit of the bacterial sodium ion pump glutaconyl-coenzyme A decarboxylase.
Wendt et al. (2003)