› 1o78

Solution NMR

Biotin carboxyl carrier domain of transcarboxylase (1.3S) [10-48] deletion mutant

Released:
DOI: 10.2210/pdb1o78/pdb
PDB entry 1o78 coloured by chain, ensemble of 20 models, front view.
PDB entry 1o78 coloured by chain, ensemble of 20 models, side view.
PDB entry 1o78 coloured by chain, ensemble of 20 models, top view.
Source organism: Propionibacterium freudenreichii subsp. shermanii
Primary publication:
NMR studies on the solution structure of a deletion mutant of the transcarboxylase biotin carrier subunit.
Jank MM, Sadowsky JD, Peikert C, Berger S
Int J Biol Macromol 30 233-42 (2002)
PMID: 12297230

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: 84 amino acids
Theoretical weight: 8.67 KDa
Source organism: Propionibacterium freudenreichii subsp. shermanii
Expression system: Escherichia coli
UniProt:
  • Canonical: P02904 (Residues: 48-123; Coverage: 62%)
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
Expression system: Escherichia coli

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