› 2zgw

X-ray diffraction
1.5Å resolution

Crystal Structure Of Biotin Protein Ligase From Pyrococcus Horikoshii Complexed with Adenosine and Biotin, Mutations R48A and K111A

Released:
DOI: 10.2210/pdb2zgw/pdb
PDB entry 2zgw coloured by chain, front view.
PDB entry 2zgw coloured by chain, side view.
PDB entry 2zgw coloured by chain, top view.
Source organism: Pyrococcus horikoshii OT3
Primary publication:
Protein biotinylation visualized by a complex structure of biotin protein ligase with a substrate.
Bagautdinov B, Matsuura Y, Bagautdinova S, Kunishima N
J Biol Chem 283 14739-50 (2008)
PMID: 18372281

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129627 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
BPL/LPL catalytic domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 235 amino acids
Theoretical weight: 25.96 KDa
Source organism: Pyrococcus horikoshii OT3
Expression system: Escherichia coli
UniProt:
  • Canonical: O57883 (Residues: 1-235; Coverage: 100%)
Gene name: PH0147
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ADN 2 x ADN
Ligand BTN 2 x BTN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B1
Spacegroup: P21
Unit cell:
a: 38.308Å b: 82.876Å c: 72.578Å
α: 90° β: 103.5° γ: 90°
R-values:
R R work R free
0.187 0.187 0.204
Expression system: Escherichia coli

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Citations

6 review citations

Modulation of epigenetic targets for anticancer therapy: clinicopathological relevance, structural data and drug discovery perspectives.
Andreoli et al. (2013)
5 more