› 3tms

X-ray diffraction
2.1Å resolution

PLASTIC ADAPTATION TOWARD MUTATIONS IN PROTEINS: STRUCTURAL COMPARISON OF THYMIDYLATE SYNTHASES

Released:
DOI: 10.2210/pdb3tms/pdb
PDB entry 3tms coloured by chain, front view.
PDB entry 3tms coloured by chain, side view.
PDB entry 3tms coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Plastic adaptation toward mutations in proteins: structural comparison of thymidylate synthases.
Perry KM, Fauman EB, Finer-Moore JS, Montfort WR, Maley GF, Maley F, Stroud RM
Proteins 8 315-33 (1990)
PMID: 2128651

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: 30.52 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

1 bound ligand:
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: I213
Unit cell:
a: 133Å b: 133Å c: 133Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.22 not available
Expression system: Not provided

Quick links

Citations

7 review citations

Tetrahydrofolate and tetrahydromethanopterin compared: functionally distinct carriers in C1 metabolism.
Maden BE. (2000)
6 more

20 mentions without citation

LIGSITEcsc: predicting ligand binding sites using the Connolly surface and degree of conservation.
Huang et al. (2006)
19 more