› 1bq2

X-ray diffraction
2.2Å resolution

E. COLI THYMIDYLATE SYNTHASE MUTANT N177A

Released:
DOI: 10.2210/pdb1bq2/pdb
PDB entry 1bq2 coloured by chain, front view.
PDB entry 1bq2 coloured by chain, side view.
PDB entry 1bq2 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Inactivity of N229A thymidylate synthase due to water-mediated effects: isolating a late stage in methyl transfer.
Reyes CL, Sage CR, Rutenber EE, Nissen RM, Finer-Moore JS, Stroud RM
J Mol Biol 284 699-712 (1998)
PMID: 9826509

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: 30.47 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 PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: I213
Unit cell:
a: 133.06Å b: 133.06Å c: 133.06Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.172 0.217
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Observation of unstable species in enzyme-catalyzed transformations using protein crystallography.
Petsko et al. (2000)
1 more

1 mention without citation

A normalized root-mean-square distance for comparing protein three-dimensional structures.
Carugo et al. (2001)