› 4lxi

X-ray diffraction
2.17Å resolution

Crystal Structure of the S105A mutant of a carbon-carbon bond hydrolase, DxnB2 from Sphingomonas wittichii RW1, in complex with 5,8-diF HOPDA

Released:
DOI: 10.2210/pdb4lxi/pdb
PDB entry 4lxi coloured by chain, front view.
PDB entry 4lxi coloured by chain, side view.
PDB entry 4lxi coloured by chain, top view.
Source organism: Rhizorhabdus wittichii RW1
Primary publication:
A substrate-assisted mechanism of nucleophile activation in a Ser-His-Asp containing C-C bond hydrolase.
Ruzzini AC, Bhowmik S, Ghosh S, Yam KC, Bolin JT, Eltis LD
Biochemistry 52 7428-38 (2013)
PMID: 24067021

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-164771 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
MCP Hydrolase Chain: A
Molecule details ›
Chain: A
Length: 277 amino acids
Theoretical weight: 30.21 KDa
Source organism: Rhizorhabdus wittichii RW1
Expression system: Escherichia coli
Structure domains: alpha/beta hydrolase

Ligands and Environments

2 bound ligands:
Ligand 22J 1 x 22J
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P6522
Unit cell:
a: 66.155Å b: 66.155Å c: 342.18Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.207 0.204 0.258
Expression system: Escherichia coli

Quick links

Citations

5 citation in other articles

How the Same Core Catalytic Machinery Catalyzes 17 Different Reactions: the Serine-Histidine-Aspartate Catalytic Triad of α/β-Hydrolase Fold Enzymes.
Rauwerdink et al. (2015)
4 more

1 mention without citation

A substrate-assisted mechanism of nucleophile activation in a Ser-His-Asp containing C-C bond hydrolase.
Ruzzini et al. (2013)