MolNFT v1 · #346215 · protein

AlphaFold monomer V2.0 prediction for ribonucleoside-diphosphate reductase 1 subunit beta (P69925)

P69925: “AlphaFold monomer V2.0 prediction for ribonucleoside-diphosphate reductase 1 subunit beta (P69925)”. 1 pocket (best druggability 0.36). MolNFT v1 #346215 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

Accession: P69925
Type: protein
Length: 376 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x46EfCa788d03A3e879DAcDb96552AB8Bbc7e20b3
Molecule: Ribonucleoside-diphosphate reductase 1 subunit beta
UniProt: P69925
Pockets: 1 · best druggability 0.36

Structure

1 distinct chain · 64% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ribonucleoside-diphosphate reductase 1 subunit beta	protein	376	64% helix, 4% strand	P69925

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	86	0.36	0.75	21	empty

Compared structures

5CI2 · Ribonucleotide reductase Y122 2,3,6-F3Y variant · an experimental structure of the same protein · chain A against A, TM-score 0.93
5CI2 · Ribonucleotide reductase Y122 2,3,6-F3Y variant · an experimental structure of the same protein · chain A against A, TM-score 0.93
5CI3 · Ribonucleotide reductase Y122 2,3,5-F3Y variant · an experimental structure of the same protein · chain A against A, TM-score 0.93
5CI3 · Ribonucleotide reductase Y122 2,3,5-F3Y variant · an experimental structure of the same protein · chain A against A, 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 P69925
Elsewhere: UniProt P69925 · AlphaFold DB P69925

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