› 5d6o

X-ray diffraction
1.8Å resolution

Orthorhombic Crystal Structure of an acetylester hydrolase from Corynebacterium glutamicum

Released:
DOI: 10.2210/pdb5d6o/pdb
PDB entry 5d6o coloured by chain, front view.
PDB entry 5d6o coloured by chain, side view.
PDB entry 5d6o coloured by chain, top view.
Source organism: Corynebacterium glutamicum ATCC 13032
Primary publication:
A novel esterase subfamily with α/β-hydrolase fold suggested by structures of two bacterial enzymes homologous to L-homoserine O-acetyl transferases.
Tölzer C, Pal S, Watzlawick H, Altenbuchner J, Niefind K
FEBS Lett 590 174-84 (2016)
PMID: 26787467

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-185656 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable esterase Cgl0839 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 349 amino acids
Theoretical weight: 38.87 KDa
Source organism: Corynebacterium glutamicum ATCC 13032
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8NS43 (Residues: 1-349; Coverage: 100%)
Gene name: Cgl0839
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

3 bound ligands:
Ligand CL 8 x CL
Ligand MG 5 x MG
Ligand GOL 17 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P212121
Unit cell:
a: 44.141Å b: 89.612Å c: 322.788Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.175 0.21
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

A Novel Subfamily Esterase with a Homoserine Transacetylase-like Fold but No Transferase Activity.
Li et al. (2017)
1 more

2 mentions without citation

Self-association of a highly charged arginine-rich cell-penetrating peptide.
Tesei et al. (2017)
1 more