› 1zs9

X-ray diffraction
1.7Å resolution

Crystal structure of human enolase-phosphatase E1

Released:
DOI: 10.2210/pdb1zs9/pdb
PDB entry 1zs9 coloured by chain, front view.
PDB entry 1zs9 coloured by chain, side view.
PDB entry 1zs9 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: 29.24 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

1 bound ligand:
Ligand MG 3 x MG
1 modified residue:
Ligand MSE 6 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: BSRF BEAMLINE 3W1A
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
0.208 0.208 0.241
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)
19 other articles

1 mention without citation

The dipeptidyl peptidase IV inhibitors vildagliptin and K-579 inhibit a phospholipase C: a case of promiscuous scaffolds in proteins.
Chakraborty et al. (2013)