1gd9

X-ray diffraction
1.8Å resolution

CRYSTALL STRUCTURE OF PYROCOCCUS PROTEIN-A1

Released:
Source organism: Pyrococcus horikoshii
Primary publication:
Temperature dependence of the enzyme-substrate recognition mechanism.
J. Biochem. 129 173-8 (2001)
PMID: 11134972

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aminotransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 389 amino acids
Theoretical weight: 43.96 KDa
Source organism: Pyrococcus horikoshii
Expression system: Escherichia coli
UniProt:
  • Canonical: O59096 (Residues: 1-389; Coverage: 100%)
Gene name: PH1371
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: P212121
Unit cell:
a: 59.67Å b: 122.28Å c: 127.17Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.213 0.21 0.242
Expression system: Escherichia coli