MolNFT v1 · #15759 · protein

Fluoride inhibition of yeast enolase: crystal structure of the enolase-MG2+-F--pi complex at 2.6-ångströms resolution

1NEL: “Fluoride inhibition of yeast enolase: crystal structure of the enolase-MG2+-F--pi complex at 2.6-ångströms…”. X-ray diffraction, 3 ligands (MG, PO4, F), 1 pocket (best druggability 0.44). MolNFT v1 #15759 on GenesisL1: 3D structure…

PDB: 1NEL
Type: protein
Length: 436 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Enolase
EC: 4.2.1.11
UniProt: P00924
Ligands: MG, PO4, F
Pockets: 1 · best druggability 0.44

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Enolase (EC 4.2.1.11)	protein	436	42% helix, 17% strand	P00924

Ligands and binding sites

MG · Magnesium ion · metal · chains A
PO4 · Phosphate ion · ion · chains A
F · Fluoride ion · ion · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	110	0.44	0.78	23	empty

Compared structures

1NEL · Fluoride inhibition of yeast enolase: crystal structure of the enolase-MG2+-F--pi complex… · the same entry in another collection · chain A against A, TM-score 1.00
P00924 · AlphaFold monomer V2.0 prediction for enolase 1 (P00924) · a predicted model of the same protein · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P00924
Elsewhere: RCSB PDB 1NEL · PDBe 1NEL · UniProt P00924

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