2e10

X-ray diffraction
1.35Å resolution

Crystal Structure Of Biotin Protein Ligase From Pyrococcus Horikoshii, Mutation R51A

Released:
Source organism: Pyrococcus horikoshii OT3
Entry authors: Bagautdinov B, Taketa M, Matsuura Y, Kunishima N, RIKEN Structural Genomics/Proteomics Initiative (RSGI)

Function and Biology Details

Reaction catalysed:
ATP + biotin + [biotin carboxyl-carrier protein]-L-lysine = AMP + diphosphate + [biotin carboxyl-carrier protein]-N(6)-biotinyl-L-lysine
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
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: 26.02 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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B1
Spacegroup: P21
Unit cell:
a: 38.298Å b: 82.654Å c: 72.424Å
α: 90° β: 103.49° γ: 90°
R-values:
R R work R free
0.209 0.209 0.225
Expression system: Escherichia coli