MolNFT v1 · #274156 · protein

AlphaFold monomer V2.0 prediction for nuclear migration protein nudc (Q9Y266)

Q9Y266: “AlphaFold monomer V2.0 prediction for nuclear migration protein nudc (Q9Y266)”. 2 pockets (best druggability 0.29). MolNFT v1 #274156 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

Accession: Q9Y266
Type: protein
Length: 331 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x417CEcD4bACa5fb5c4B2864EA1ebdFD915Ff5dDA
Molecule: Nuclear migration protein nudc
UniProt: Q9Y266
Pockets: 2 · best druggability 0.29

Structure

1 distinct chain · 45% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nuclear migration protein nudc	protein	331	45% helix, 15% strand	Q9Y266

Pockets

2 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	71	0.29	0.72	12	empty
2	70	0.27	0.72	10	empty

Compared structures

3QOR · Crystal structure of human nuclear migration protein NudC · an experimental structure of the same protein · chain A against B, TM-score 0.35
3QOR · Crystal structure of human nuclear migration protein nudc · an experimental structure of the same protein · chain A against B, TM-score 0.35
7NDX · Crystal structure of the human HSP40 DNAJB1-ctds in complex with a peptide of nudc · an experimental structure of the same protein · chain A against B, TM-score 0.08
7NDX · Crystal structure of the human HSP40 DNAJB1-CTDs in complex with a peptide of NudC · an experimental structure of the same protein · chain A against B, TM-score 0.08

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 Q9Y266
Elsewhere: UniProt Q9Y266 · AlphaFold DB Q9Y266

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