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The enth domain from epsin-1

Analyse The enth domain from epsin-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5ONF
Type: protein
Length: 441 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Epsin-1
UniProt: Q12518
Pockets: 6 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 67% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Epsin-1	protein	147	67% helix, 0% strand	Q12518

Ligands and binding sites

MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	296	0.68	0.83	42	empty
2	297	0.60	0.78	27	empty
3	210	0.50	0.76	26	empty
4	209	0.49	0.76	21	empty
5	91	0.42	0.78	23	empty

Interfaces

2 interfaces between chains.

A–C · 813 Å² buried · 7 hydrogen bonds · protein-protein
A–B · 546 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

5ONF · The ENTH domain from epsin-1 · the same entry in another collection · chain A against A, TM-score 1.00
Q12518 · AlphaFold monomer V2.0 prediction for epsin-1 (Q12518) · a predicted model of the same protein · chain B against A, TM-score 0.92

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 Q12518
Elsewhere: RCSB PDB 5ONF · PDBe 5ONF · UniProt Q12518

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