3elb

X-ray diffraction
2Å resolution

Human CTP: Phosphoethanolamine Cytidylyltransferase in complex with CMP

Released:
Source organism: Homo sapiens
Entry authors: Karlberg T, Welin M, Andersson J, Arrowsmith CH, Berglund H, Bountra C, Collins R, Dahlgren LG, Edwards AM, Flodin S, Flores A, Graslund S, Hammarstrom M, Johansson A, Johansson I, Kotenyova T, Lehtio L, Moche M, Nilsson ME, Nordlund P, Nyman T, Persson C, Sagemark J, Thorsell AG, Tresaugues L, Van Den Berg S, Weigelt J, Wikstrom M, Wisniewska M, Schuler H, Structural Genomics Consortium (SGC)

Function and Biology Details

Reaction catalysed:
CTP + ethanolamine phosphate = diphosphate + CDP-ethanolamine
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
PDBe Complex ID:
PDB-CPX-189197 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ethanolamine-phosphate cytidylyltransferase Chain: A
Molecule details ›
Chain: A
Length: 341 amino acids
Theoretical weight: 39.12 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q99447 (Residues: 18-356; Coverage: 87%)
Gene name: PCYT2
Sequence domains: Cytidylyltransferase-like
Structure domains: HUPs

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P41212
Unit cell:
a: 74.179Å b: 74.179Å c: 139.723Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.196 0.242
Expression system: Escherichia coli