X-ray diffraction
2.2Å resolution

Crystal Structure of human Enolase 1

Source organism: Homo sapiens
Primary publication:
Structure of human alpha-enolase (hENO1), a multifunctional glycolytic enzyme.
Acta Crystallogr. D Biol. Crystallogr. 64 651-7 (2008)
PMID: 18560153

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Alpha-enolase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 433 amino acids
Theoretical weight: 47.1 KDa
Source organism: Homo sapiens
  • Canonical: P06733 (Residues: 2-434; Coverage: 100%)
Gene names: ENO1, ENO1L1, MBPB1, MPB1
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 4A
Spacegroup: P42
Unit cell:
a: 192.796Å b: 192.796Å c: 65.17Å
α: 90° β: 90° γ: 90°
R R work R free
0.187 0.184 0.217