MolNFT v1 · #161680 · protein

Idol ferm domain

6QLY · E3 ubiquitin-protein ligase mylip: “Idol ferm domain”. X-ray diffraction, 1 ligand (SO4), 1 pocket (best druggability 0.75). MolNFT v1 #161680 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6QLY
Type: protein
Length: 330 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: E3 ubiquitin-protein ligase mylip
EC: 2.3.2.27
UniProt: Q8WY64
Ligands: SO4
Pockets: 1 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	E3 ubiquitin-protein ligase mylip (EC 2.3.2.27)	protein	330	40% helix, 19% strand	Q8WY64

Ligands and binding sites

SO4 · Sulfate ion · ion · chains A
EDO · 1,2-ethanediol · additive · 2 copies · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	654	0.75	0.81	80	SO4

Compared structures

6QLY · IDOL FERM domain · the same entry in another collection · chain A against A, TM-score 1.00
Q8WY64 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase mylip (Q8WY64) · a predicted model of the same protein · chain A against A, TM-score 0.84

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 Q8WY64
Elsewhere: RCSB PDB 6QLY · PDBe 6QLY · UniProt Q8WY64

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