› 2jbw

X-ray diffraction
2.1Å resolution

Crystal Structure of the 2,6-dihydroxy-pseudo-oxynicotine Hydrolase.

Released:
DOI: 10.2210/pdb2jbw/pdb
PDB entry 2jbw coloured by chain, front view.
PDB entry 2jbw coloured by chain, side view.
PDB entry 2jbw coloured by chain, top view.
Source organism: Paenarthrobacter nicotinovorans
Primary publication:
Structure and action of a C-C bond cleaving alpha/beta-hydrolase involved in nicotine degradation.
Schleberger C, Sachelaru P, Brandsch R, Schulz GE
J Mol Biol 367 409-18 (2007)
PMID: 17275835

Function and Biology Details

Reaction catalysed: 
1-(2,6-dihydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H(2)O = 2,6-dihydroxypyridine + 4-methylaminobutanoate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188103 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2,6-dihydropseudooxynicotine hydrolase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 386 amino acids
Theoretical weight: 43.86 KDa
Source organism: Paenarthrobacter nicotinovorans
Expression system: Escherichia coli
UniProt:
  • Canonical: Q93NG6 (Residues: 1-365; Coverage: 100%)
Sequence domains: Esterase FrsA-like
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand NA 4 x NA
1 modified residue:
Ligand MSE 56 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P21
Unit cell:
a: 90.57Å b: 57.02Å c: 152.697Å
α: 90° β: 103.35° γ: 90°
R-values:
R R work R free
0.183 0.181 0.238
Expression system: Escherichia coli

Quick links

Citations

1 review citation

The enzymes of microbial nicotine metabolism.
Fitzpatrick PF. (2018)
11 other articles

2 mentions without citation

Catalytic and structural properties of pheophytinase, the phytol esterase involved in chlorophyll breakdown.
Guyer et al. (2018)
1 more