› 6d3q

X-ray diffraction
2.24Å resolution

Crystal structure of Escherichia coli enolase complexed with a natural inhibitor SF2312.

Released:
DOI: 10.2210/pdb6d3q/pdb
PDB entry 6d3q coloured by chain, front view.
PDB entry 6d3q coloured by chain, side view.
PDB entry 6d3q coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Functional and structural basis of E. coli enolase inhibition by SF2312: a mimic of the carbanion intermediate.
Krucinska J, Lombardo MN, Erlandsen H, Hazeen A, Duay SS, Pattis JG, Robinson VL, May ER, Wright DL
Sci Rep 9 17106 (2019)
PMID: 31745118

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141412 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Enolase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 439 amino acids
Theoretical weight: 46.46 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6P9 (Residues: 1-432; Coverage: 100%)
Gene names: JW2750, b2779, eno
Sequence domains:

Ligands and Environments

4 bound ligands:
Ligand 4NG 6 x 4NG
Ligand MG 12 x MG
Ligand GOL 5 x GOL
Ligand SO4 12 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P212121
Unit cell:
a: 104.751Å b: 142.071Å c: 207.28Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.163 0.216
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Beyond ENO1, emerging roles and targeting strategies of other enolases in cancers.
Ni et al. (2023)
4 other articles

1 mention without citation

Functional and structural basis of E. coli enolase inhibition by SF2312: a mimic of the carbanion intermediate.
Krucinska et al. (2019)