PDBe 1pdz

X-ray diffraction
2.2Å resolution

X-RAY STRUCTURE AND CATALYTIC MECHANISM OF LOBSTER ENOLASE

Released:
Source organism: Homarus gammarus
Primary publication:
X-ray structure and catalytic mechanism of lobster enolase.
Biochemistry 34 12513-23 (1995)
PMID: 7547999

Function and Biology Details

Reaction catalysed:
2-phospho-D-glycerate = phosphoenolpyruvate + H(2)O
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Enolase Chain: A
Molecule details ›
Chain: A
Length: 434 amino acids
Theoretical weight: 47.12 KDa
Source organism: Homarus gammarus
UniProt:
  • Canonical: P56252 (Residues: 1-433; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LURE BEAMLINE DW32
Spacegroup: P3121
Unit cell:
a: 110.8Å b: 110.8Å c: 73.4Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.215 0.215 not available