› 4ao8

X-ray diffraction
1.61Å resolution

PEG-bound complex of a novel cold-adapted esterase from an Arctic intertidal metagenomic library

Released:
DOI: 10.2210/pdb4ao8/pdb
PDB entry 4ao8 coloured by chain, front view.
PDB entry 4ao8 coloured by chain, side view.
PDB entry 4ao8 coloured by chain, top view.
Source organism: unidentified
Primary publication:
Functional and structural studies of a novel cold-adapted esterase from an Arctic intertidal metagenomic library.
Fu J, Leiros HK, de Pascale D, Johnson KA, Blencke HM, Landfald B
Appl Microbiol Biotechnol 97 3965-78 (2013)
PMID: 22832985

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-164286 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ESTERASE Chain: A
Molecule details ›
Chain: A
Length: 259 amino acids
Theoretical weight: 28.29 KDa
Source organism: unidentified
Expression system: Escherichia coli K-12
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
Ligand PEG 1 x PEG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P21212
Unit cell:
a: 55.97Å b: 69.719Å c: 53.982Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.178 0.212
Expression system: Escherichia coli K-12

Quick links

Citations

7 review citations

Alternative hosts for functional (meta)genome analysis.
Liebl et al. (2014)
6 more

1 mention without citation

Cold-Active Lipases and Esterases: A Review on Recombinant Overexpression and Other Essential Issues.
Matinja et al. (2022)