› 1yns

X-ray diffraction
1.7Å resolution

Crystal Structure Of Human Enolase-phosphatase E1 and its complex with a substrate analog

Released:
DOI: 10.2210/pdb1yns/pdb
PDB entry 1yns coloured by chain, front view.
PDB entry 1yns coloured by chain, side view.
PDB entry 1yns coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of human E1 enzyme and its complex with a substrate analog reveals the mechanism of its phosphatase/enolase activity.
Wang H, Pang H, Bartlam M, Rao Z
J Mol Biol 348 917-26 (2005)
PMID: 15843022

Function and Biology Details

Reaction catalysed: 
(1a) 5-(methylsulfanyl)-2,3-dioxopentyl phosphate = 2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-enyl phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193772 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Enolase-phosphatase E1 Chain: A
Molecule details ›
Chain: A
Length: 261 amino acids
Theoretical weight: 28.96 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9UHY7 (Residues: 1-261; Coverage: 100%)
Gene names: ENOPH1, MASA, MSTP145
Sequence domains: haloacid dehalogenase-like hydrolase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MG 3 x MG
Ligand HPO 1 x HPO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P212121
Unit cell:
a: 54.017Å b: 57.546Å c: 87.318Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.256 0.225 0.234
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Metabolic characteristics and importance of the universal methionine salvage pathway recycling methionine from 5'-methylthioadenosine.
Albers E. (2009)
18 other articles

2 mentions without citation

Crystal structure of ED-Eya2: insight into dual roles as a protein tyrosine phosphatase and a transcription factor.
Jung et al. (2010)
1 more