› 1b02

X-ray diffraction
2.5Å resolution

CRYSTAL STRUCTURE OF THYMIDYLATE SYNTHASE A FROM BACILLUS SUBTILIS

Released:
DOI: 10.2210/pdb1b02/pdb
PDB entry 1b02 coloured by chain, front view.
PDB entry 1b02 coloured by chain, side view.
PDB entry 1b02 coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Crystal structure of thymidylate synthase A from Bacillus subtilis.
Fox KM, Maley F, Garibian A, Changchien LM, Van Roey P
Protein Sci 8 538-44 (1999)
PMID: 10091656

Function and Biology Details

Reaction catalysed: 
5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-143506 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thymidylate synthase 1 Chain: A
Molecule details ›
Chain: A
Length: 279 amino acids
Theoretical weight: 32.85 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CI79 (Residues: 1-279; Coverage: 100%)
Gene names: BSU17680, thyA1
Sequence domains: Thymidylate synthase
Structure domains: Thymidylate synthase/dCMP hydroxymethylase domain

Ligands and Environments


Cofactor: Ligand C2F 1 x C2F
1 bound ligand:
Ligand UFP 1 x UFP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 55.57Å b: 105.01Å c: 117.26Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.194 0.233
Expression system: Escherichia coli

Quick links

Citations

12 citation in other articles

Analysis of the residue-residue coevolution network and the functionally important residues in proteins.
Lee et al. (2008)
11 more

6 mentions without citation

Differential requirements for FcγR engagement by protective antibodies against Ebola virus.
Bournazos et al. (2019)
5 more