› 7pen

X-ray diffraction
1.6Å resolution

Crystal Structure of Two-Domain Laccase mutant Y230A from Streptomyces griseoflavus

Released:
DOI: 10.2210/pdb7pen/pdb
PDB entry 7pen coloured by chain, front view.
PDB entry 7pen coloured by chain, side view.
PDB entry 7pen coloured by chain, top view.
Source organism: Streptomyces griseoflavus
Primary publication:
Engineering the Catalytic Properties of Two-Domain Laccase from Streptomyces griseoflavus Ac-993.
Kolyadenko I, Scherbakova A, Kovalev K, Gabdulkhakov A, Tishchenko S
Int J Mol Sci 23 (2021)
PMID: 35008493

Function and Biology Details

Reaction catalysed: 
4 benzenediol + O(2) = 4 benzosemiquinone + 2 H(2)O
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Two-domain laccase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 322 amino acids
Theoretical weight: 34.66 KDa
Source organism: Streptomyces griseoflavus
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A0M4FJ81 (Residues: 1-322; Coverage: 100%)
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand CU 24 x CU
Ligand NA 2 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P21
Unit cell:
a: 77.26Å b: 94.98Å c: 116.27Å
α: 90° β: 91.667° γ: 90°
R-values:
R R work R free
0.136 0.135 0.165
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

Does Tyrosine Protect S. coelicolor Laccase from Oxidative Degradation or Act as an Extended Catalytic Site?
Kielb et al. (2022)
3 more

1 mention without citation

Engineering the Catalytic Properties of Two-Domain Laccase from Streptomyces griseoflavus Ac-993.
Kolyadenko et al. (2021)