MolNFT v1 · #379453 · protein

AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase RMD5 (Q12508)

Q12508: “AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase RMD5 (Q12508)”. 4 pockets (best druggability 0.40). MolNFT v1 #379453 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

Accession: Q12508
Type: protein
Length: 421 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x79a905d858Ce72991FD6E7a9C6498620f42E146D
Molecule: E3 ubiquitin-protein ligase RMD5
UniProt: Q12508
Pockets: 4 · best druggability 0.40

Structure

1 distinct chain · 66% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	E3 ubiquitin-protein ligase RMD5	protein	421	66% helix, 5% strand	Q12508

Pockets

4 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	164	0.40	0.72	18	empty
2	93	0.38	0.76	18	empty
3	53	0.32	0.77	12	empty
4	54	0.30	0.75	15	empty

Compared structures

8PMQ · Catalytic module of yeast GID E3 ligase bound to multiphosphorylated Ubc8~ubiquitin · an experimental structure of the same protein · chain A against 2, TM-score 0.49
7NS4 · Catalytic module of yeast chelator-gid SR4 E3 ubiquitin ligase · an experimental structure of the same protein · chain A against b, TM-score 0.46
7NS4 · Catalytic module of yeast Chelator-GID SR4 E3 ubiquitin ligase · an experimental structure of the same protein · chain A against b, TM-score 0.46

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 Q12508
Elsewhere: UniProt Q12508 · AlphaFold DB Q12508

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