› 1p43

X-ray diffraction
1.8Å resolution

REVERSE PROTONATION IS THE KEY TO GENERAL ACID-BASE CATALYSIS IN ENOLASE

Released:
DOI: 10.2210/pdb1p43/pdb
PDB entry 1p43 coloured by chain, front view.
PDB entry 1p43 coloured by chain, side view.
PDB entry 1p43 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Reverse protonation is the key to general acid-base catalysis in enolase.
Sims PA, Larsen TM, Poyner RR, Cleland WW, Reed GH
Biochemistry 42 8298-306 (2003)
PMID: 12846578

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
Molecule details ›
Chains: A, B
Length: 436 amino acids
Theoretical weight: 46.73 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
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 4 x MG
Ligand 2PG 2 x 2PG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR591
Spacegroup: P21212
Unit cell:
a: 107.3Å b: 115.1Å c: 72.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.185 0.213
Expression system: Escherichia coli

Quick links

Citations

4 review citations

A twisted base? The role of arginine in enzyme-catalyzed proton abstractions.
Guillén Schlippe et al. (2005)
3 more

2 mentions without citation

Discrete-continuous duality of protein structure space.
Sadreyev et al. (2009)
1 more