› 1pdy

X-ray diffraction
2.4Å resolution

X-RAY STRUCTURE AND CATALYTIC MECHANISM OF LOBSTER ENOLASE

Released:
DOI: 10.2210/pdb1pdy/pdb
PDB entry 1pdy coloured by chain, front view.
PDB entry 1pdy coloured by chain, side view.
PDB entry 1pdy coloured by chain, top view.
Source organism: Homarus gammarus
Primary publication:
X-ray structure and catalytic mechanism of lobster enolase.
Duquerroy S, Camus C, Janin J
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:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157443 (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

1 bound ligand:
Ligand SO4 1 x SO4
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

Quick links

Citations

3 review citations

Glycolysis as a target for the design of new anti-trypanosome drugs.
Verlinde et al. (2001)
2 more

9 mentions without citation

LIGSITEcsc: predicting ligand binding sites using the Connolly surface and degree of conservation.
Huang et al. (2006)
8 more