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AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase RNF123 (Q5XPI4)

Analyse AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase RNF123… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: Q5XPI4
Type: protein
Length: 1,314 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0xbDA05C32aD6eE153C8C5A78dfa48d7Ba25694fea
Molecule: E3 ubiquitin-protein ligase RNF123
UniProt: Q5XPI4
Pockets: 20 · best druggability 0.84

Structure

1 distinct chain · 50% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	E3 ubiquitin-protein ligase RNF123	protein	1314	50% helix, 9% strand	Q5XPI4

Pockets

20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	855	0.84	0.86	88	empty
2	770	0.71	0.77	71	empty
3	201	0.65	0.84	28	empty
4	106	0.56	0.84	17	empty
5	338	0.56	0.75	41	empty

Compared structures

2MA6 · Solution NMR Structure of the RING finger domain from the Kip1 ubiquitination-promoting… · an experimental structure of the same protein · chain A against A, TM-score 0.04
2MA6 · Solution NMR structure of the ring finger domain from the KIP1 ubiquitination-promoting… · an experimental structure of the same protein · chain A against A, TM-score 0.04

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 Q5XPI4
Elsewhere: UniProt Q5XPI4 · AlphaFold DB Q5XPI4

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