› 1tsn

X-ray diffraction
2.2Å resolution

THYMIDYLATE SYNTHASE TERNARY COMPLEX WITH FDUMP AND METHYLENETETRAHYDROFOLATE

Released:
DOI: 10.2210/pdb1tsn/pdb
PDB entry 1tsn coloured by chain, front view.
PDB entry 1tsn coloured by chain, side view.
PDB entry 1tsn coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Use of strain in a stereospecific catalytic mechanism: crystal structures of Escherichia coli thymidylate synthase bound to FdUMP and methylenetetrahydrofolate.
Hyatt DC, Maley F, Montfort WR
Biochemistry 36 4585-94 (1997)
PMID: 9109668

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141681 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thymidylate synthase Chain: A
Molecule details ›
Chain: A
Length: 264 amino acids
Theoretical weight: 30.56 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
  • Canonical: P0A884 (Residues: 1-264; Coverage: 100%)
Gene names: JW2795, b2827, thyA
Sequence domains: Thymidylate synthase
Structure domains: Thymidylate synthase/dCMP hydroxymethylase domain

Ligands and Environments


Cofactor: Ligand C2F 1 x C2F
2 bound ligands:
Ligand PO4 1 x PO4
Ligand UFP 1 x UFP
1 modified residue:
Ligand CXM 1 x CXM

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR571
Spacegroup: P3121
Unit cell:
a: 72.1Å b: 72.1Å c: 115.27Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.178 0.178 not available
Expression system: Not provided

Quick links

Citations

3 review citations

Tethering: fragment-based drug discovery.
Erlanson et al. (2004)
2 more

12 mentions without citation

Thermodynamic and NMR Assessment of Ligand Cooperativity and Intersubunit Communication in Symmetric Dimers: Application to Thymidylate Synthase.
Lee et al. (2018)
11 more