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Crystal structure of ENOLASE1

Analyse Crystal structure of ENOLASE1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2PSN
Type
protein
Length
1,728 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Alpha-enolase
EC
4.2.1.11
UniProt
P06733
Ligands
MG, PO4
Pockets
14 · best druggability 0.74

Structure

x-ray diffraction · 3 distinct chains · 45% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BAlpha-enolase (EC 4.2.1.11)protein43244% helix, 17% strandP06733
CAlpha-enolase (EC 4.2.1.11)protein43345% helix, 17% strandP06733
DAlpha-enolase (EC 4.2.1.11)protein43144% helix, 17% strandP06733

Ligands and binding sites

  • MG · Magnesium ion · metal · 8 copies · chains A, B, C, D
  • PO4 · Phosphate ion · ion · 4 copies · chains A, B, C, D

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

14 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110440.740.7761empty
210560.740.7759empty
34720.670.7966empty
42260.560.7933empty
52460.560.7835empty

Interfaces

3 interfaces between chains.

  • C–D · 2130 Ų buried · 44 hydrogen bonds · protein-protein
  • A–B · 2071 Ų buried · 45 hydrogen bonds · protein-protein
  • B–D · 713 Ų buried · 8 hydrogen bonds · protein-protein

Compared structures

  • 2PSN · Crystal structure of enolase1 · the same entry in another collection · chain D against D, TM-score 1.00
  • P06733 · AlphaFold monomer V2.0 prediction for alpha-enolase (P06733) · a predicted model of the same protein · chain D against A, TM-score 1.00

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