› 3v48

X-ray diffraction
2.1Å resolution

Crystal Structure of the putative alpha/beta hydrolase RutD from E.coli

Released:
DOI: 10.2210/pdb3v48/pdb
PDB entry 3v48 coloured by chain, front view.
PDB entry 3v48 coloured by chain, side view.
PDB entry 3v48 coloured by chain, top view.
Source organism: Escherichia coli SE11
Primary publication:
A multi-faceted analysis of RutD reveals a novel family of α/β hydrolases.
Knapik AA, Petkowski JJ, Otwinowski Z, Cymborowski MT, Cooper DR, Majorek KA, Chruszcz M, Krajewska WM, Minor W
Proteins 80 2359-68 (2012)
PMID: 22641504

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-110342 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Putative carbamate hydrolase RutD Chains: A, B
Molecule details ›
Chains: A, B
Length: 268 amino acids
Theoretical weight: 29.4 KDa
Source organism: Escherichia coli SE11
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: B6I985 (Residues: 1-266; Coverage: 100%)
Gene names: ECSE_1071, rutD
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

2 bound ligands:
Ligand GOL 4 x GOL
Ligand SCN 3 x SCN
1 modified residue:
Ligand MSE 12 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P43212
Unit cell:
a: 79.597Å b: 79.597Å c: 161.753Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.169 0.226
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 citation in other articles

ESTHER, the database of the α/β-hydrolase fold superfamily of proteins: tools to explore diversity of functions.
Lenfant et al. (2013)
3 more

1 mention without citation

A multi-faceted analysis of RutD reveals a novel family of α/β hydrolases.
Knapik et al. (2012)