› 1ev5

X-ray diffraction
1.7Å resolution

CRYSTAL STRUCTURE ANALYSIS OF ALA167 MUTANT OF ESCHERICHIA COLI

Released:
DOI: 10.2210/pdb1ev5/pdb
PDB entry 1ev5 coloured by chain, front view.
PDB entry 1ev5 coloured by chain, side view.
PDB entry 1ev5 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Catalytic cysteine of thymidylate synthase is activated upon substrate binding.
Phan J, Mahdavian E, Nivens MC, Minor W, Berger S, Spencer HT, Dunlap RB, Lebioda L
Biochemistry 39 6969-78 (2000)
PMID: 10841779

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: 30.77 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
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 SO4 3 x SO4
2 modified residues:
Ligand CXM 1 x CXM
Ligand CME 3 x CME

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: I213
Unit cell:
a: 132.491Å b: 132.491Å c: 132.491Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.199 0.219
Expression system: Escherichia coli

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Citations

1 review citation

The cysteine proteome.
Go et al. (2015)
14 other articles

2 mentions without citation

A robust bulk-solvent correction and anisotropic scaling procedure.
Afonine et al. (2005)
1 more