8gyx

Electron Microscopy
3.7Å resolution

Cryo-EM structure of human CEPT1

Released:
Source organism: Homo sapiens
Related structures: EMD-34379

Function and Biology Details

Reactions catalysed:
CDP-ethanolamine + 1,2-diacyl-sn-glycerol = CMP + a phosphatidylethanolamine
CDP-choline + 1,2-diacyl-sn-glycerol = CMP + a phosphatidylcholine
CDP-choline + 1-alkenyl-2-acylglycerol = CMP + plasmenylcholine

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-195367 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Choline/ethanolaminephosphotransferase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 380 amino acids
Theoretical weight: 42.7 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: Q9Y6K0 (Residues: 28-407; Coverage: 91%)
Gene names: CEPT1, PRO1101
Sequence domains: CDP-alcohol phosphatidyltransferase

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.7Å
Relevant EMDB volumes: EMD-34379
Expression system: Homo sapiens