› 1tsw

X-ray diffraction
2.5Å resolution

THYMIDYLATE SYNTHASE R179A MUTANT

Released:
DOI: 10.2210/pdb1tsw/pdb
Model geometry
Fit model/data
Data not deposited
PDB entry 1tsw coloured by chain, front view.
PDB entry 1tsw coloured by chain, side view.
PDB entry 1tsw coloured by chain, top view.
Source organism: Lacticaseibacillus casei
Primary publication:
Contribution of a salt bridge to binding affinity and dUMP orientation to catalytic rate: mutation of a substrate-binding arginine in thymidylate synthase.
Finer-Moore JS, Fauman EB, Morse RJ, Santi DV, Stroud RM
Protein Eng 9 69-75 (1996)
PMID: 9053905

Function and Biology Details

Reaction catalysed: 
dUMP + (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate = 7,8-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-132544 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thymidylate synthase Chain: A
Molecule details ›
Chain: A
Length: 316 amino acids
Theoretical weight: 36.54 KDa
Source organism: Lacticaseibacillus casei
Expression system: Escherichia coli
UniProt:
  • Canonical: P00469 (Residues: 1-316; Coverage: 100%)
Gene name: 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

wwPDB Validation report is not available for this entry.
X-ray source: RIGAKU RU200
Spacegroup: P6122
Unit cell:
a: 78.3Å b: 78.3Å c: 243.2Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.18 0.18 not available
Expression system: Escherichia coli

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Citations

2 citation in other articles

A proposed signaling motif for nuclear import in mRNA processing via the formation of arginine claw.
Hamelberg et al. (2007)
1 more