› 1peh

Solution NMR

NMR STRUCTURE OF THE MEMBRANE-BINDING DOMAIN OF CTP PHOSPHOCHOLINE CYTIDYLYLTRANSFERASE, 10 STRUCTURES

Released:
DOI: 10.2210/pdb1peh/pdb
PDB entry 1peh coloured by chain, ensemble of 10 models, front view.
PDB entry 1peh coloured by chain, ensemble of 10 models, side view.
PDB entry 1peh coloured by chain, ensemble of 10 models, top view.
Source organism: Rattus norvegicus
Primary publication:
Structure of the membrane binding domain of CTP:phosphocholine cytidylyltransferase.
Dunne SJ, Cornell RB, Johnson JE, Glover NR, Tracey AS
Biochemistry 35 11975-84 (1996)
PMID: 8810902

Function and Biology Details

Reaction catalysed: 
CTP + phosphocholine = diphosphate + CDP-choline
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148761 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Choline-phosphate cytidylyltransferase A Chain: A
Molecule details ›
Chain: A
Length: 35 amino acids
Theoretical weight: 4.15 KDa
Source organism: Rattus norvegicus
Expression system: Not provided
UniProt:
  • Canonical: P19836 (Residues: 236-268; Coverage: 9%)
Gene names: Ctpct, Pcyt1, Pcyt1a

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: RESTRAINED DISTANCE GEOMETRY
Expression system: Not provided

Quick links

Citations

9 review citations

Amphitropic proteins: regulation by reversible membrane interactions (review).
Johnson et al. (1999)
8 more

3 mentions without citation

Disease-linked mutations in the phosphatidylcholine regulatory enzyme CCTα impair enzymatic activity and fold stability.
Cornell et al. (2019)
2 more