› 1lqa

X-ray diffraction
1.6Å resolution

TAS PROTEIN FROM ESCHERICHIA COLI IN COMPLEX WITH NADPH

Released:
DOI: 10.2210/pdb1lqa/pdb
PDB entry 1lqa coloured by chain, front view.
PDB entry 1lqa coloured by chain, side view.
PDB entry 1lqa coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of Escherichia coli protein ybgI, a toroidal structure with a dinuclear metal site.
Ladner JE, Obmolova G, Teplyakov A, Howard AJ, Khil PP, Camerini-Otero RD, Gilliland GL
BMC Struct Biol 3 7 (2003)
PMID: 14519207

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-141926 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein tas Chains: A, B
Molecule details ›
Chains: A, B
Length: 346 amino acids
Theoretical weight: 38.54 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A9T4 (Residues: 1-346; Coverage: 100%)
Gene names: JW2802, b2834, tas, ygdS
Sequence domains: Aldo/keto reductase family
Structure domains: NADP-dependent oxidoreductase domain

Ligands and Environments

1 bound ligand:
Ligand NDP 2 x NDP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P212121
Unit cell:
a: 58.3Å b: 81.46Å c: 145.02Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.146 0.145 0.186
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Beyond structural genomics: computational approaches for the identification of ligand binding sites in protein structures.
Ghersi et al. (2011)
13 other articles

3 mentions without citation

Autonomous aggregation suppression by acidic residues explains why chaperones favour basic residues.
Houben et al. (2020)
2 more