› 5lfz

X-ray diffraction
1.56Å resolution

T48 deacetylase

Released:
DOI: 10.2210/pdb5lfz/pdb
PDB entry 5lfz coloured by chain, front view.
PDB entry 5lfz coloured by chain, side view.
PDB entry 5lfz coloured by chain, top view.
Source organism: Arthrobacter sp. AW19M34-1
Primary publication:
Structure and function of a CE4 deacetylase isolated from a marine environment.
Tuveng TR, Rothweiler U, Udatha G, Vaaje-Kolstad G, Smalås A, Eijsink VGH
PLoS One 12 e0187544 (2017)
PMID: 29107991

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-165957 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ArCE4A Chain: A
Molecule details ›
Chain: A
Length: 223 amino acids
Theoretical weight: 25.03 KDa
Source organism: Arthrobacter sp. AW19M34-1
Expression system: Escherichia coli
Structure domains: Glycoside hydrolase/deacetylase

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P212121
Unit cell:
a: 39.09Å b: 56.77Å c: 76.86Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.178 0.205
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Enzymatic Modifications of Chitin, Chitosan, and Chitooligosaccharides.
Kaczmarek et al. (2019)
1 more

8 mentions without citation

Chitin Deacetylases: Structures, Specificities, and Biotech Applications.
Grifoll-Romero et al. (2018)
7 more