Research workbench

AlphaFold monomer V2.0 prediction for enolase (P37869)

Analyse AlphaFold monomer V2.0 prediction for enolase (P37869) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: P37869
Type: protein
Length: 430 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0xb3c0C983Fc44934AC589D7131C08a72544EBB92E
Molecule: Enolase
UniProt: P37869
Pockets: 3 · best druggability 0.33

Structure

1 distinct chain · 43% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Enolase	protein	430	43% helix, 20% strand	P37869

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	55	0.33	0.78	18	empty
2	95	0.32	0.73	17	empty
3	53	0.29	0.76	16	empty

Compared structures

4A3R · Crystal structure of enolase from bacillus subtilis. · an experimental structure of the same protein · chain A against D, TM-score 0.99
4A3R · Crystal structure of Enolase from Bacillus subtilis. · an experimental structure of the same protein · chain A against D, TM-score 0.99
7XML · Cryo-EM structure of peip-BS_ENOLASE complex · an experimental structure of the same protein · chain A against B, TM-score 0.93
7XML · Cryo-EM structure of PEIP-Bs_enolase complex · an experimental structure of the same protein · chain A against B, TM-score 0.93

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 P37869
Elsewhere: UniProt P37869 · AlphaFold DB P37869

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