6a9b

X-ray diffraction
2.01Å resolution

T4 dCMP hydroxymethylase structure solved by I-SAD using a home source

Released:
Model geometry
Fit model/data

Function and Biology Details

Reaction catalysed:
5,10-methylenetetrahydrofolate + H(2)O + deoxycytidylate = tetrahydrofolate + 5-hydroxymethyldeoxycytidylate
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-140376 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Deoxycytidylate 5-hydroxymethyltransferase Chain: A
Molecule details ›
Chain: A
Length: 246 amino acids
Theoretical weight: 28.52 KDa
Source organism: Escherichia virus T4
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P08773 (Residues: 1-246; Coverage: 100%)
Gene name: 42
Sequence domains: Thymidylate synthase
Structure domains: Thymidylate synthase/dCMP hydroxymethylase domain

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: RIGAKU
Spacegroup: I222
Unit cell:
a: 52.603Å b: 74.982Å c: 155.345Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.163 0.16 0.192
Expression system: Escherichia coli BL21(DE3)