› 1l8p

X-ray diffraction
2.1Å resolution

Mg-phosphonoacetohydroxamate complex of S39A yeast enolase 1

Released:
DOI: 10.2210/pdb1l8p/pdb
PDB entry 1l8p coloured by chain, front view.
PDB entry 1l8p coloured by chain, side view.
PDB entry 1l8p coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Functional and structural changes due to a serine to alanine mutation in the active-site flap of enolase.
Poyner RR, Larsen TM, Wong SW, Reed GH
Arch Biochem Biophys 401 155-63 (2002)
PMID: 12054465

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-133690 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Enolase 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 436 amino acids
Theoretical weight: 46.72 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P00924 (Residues: 2-437; Coverage: 100%)
Gene names: ENO1, ENOA, G9160, HSP48, YGR254W
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MG 8 x MG
Ligand PAH 4 x PAH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21
Unit cell:
a: 63.2Å b: 164.1Å c: 84.6Å
α: 90° β: 90.4° γ: 90°
R-values:
R R work R free
0.181 0.181 0.223
Expression system: Escherichia coli BL21(DE3)

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Citations

16 citation in other articles

Ab initio quantum mechanical/molecular mechanical molecular dynamics simulation of enzyme catalysis: the case of histone lysine methyltransferase SET7/9.
Wang et al. (2007)
15 more

1 mention without citation

Substrate-to-Product Conversion Facilitates Active Site Loop Opening in Yeast Enolase: A Molecular Dynamics Study.
Li et al. (2019)