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MolNFT v1 · #134713 · protein

Structure of human enolase 2

5TD9 · Gamma-enolase: “Structure of human enolase 2”. X-ray diffraction, 2 ligands (MG, CL), 8 pockets (best druggability 0.74). MolNFT v1 #134713 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
5TD9
Type
protein
Length
868 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Gamma-enolase
EC
4.2.1.11
UniProt
P09104
Ligands
MG, CL
Pockets
8 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BGamma-enolase (EC 4.2.1.11)protein43444% helix, 16% strandP09104

Ligands and binding sites

  • MG · Magnesium ion · metal · 2 copies · chains A, B
  • CL · Chloride ion · ion · 2 copies · chains A, B

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

Pockets

8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110300.740.7759empty
24040.640.7860CL
33770.600.7753CL
4670.430.8216empty
5820.410.7921empty

Interfaces

1 interface between chains.

  • A–B · 1903 Ų buried · 41 hydrogen bonds · protein-protein

Compared structures

  • P09104 · AlphaFold monomer V2.0 prediction for gamma-enolase (P09104) · a predicted model of the same protein · chain B against A, TM-score 0.99

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