Research workbench

AlphaFold monomer V2.0 prediction for nucleolar protein 6 (Q9H6R4)

Analyse AlphaFold monomer V2.0 prediction for nucleolar protein 6 (Q9H6R4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: Q9H6R4
Type: protein
Length: 1,146 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0xF8cD1d8d93E9783063700De244A6e3cf6A195579
Molecule: Nucleolar protein 6
UniProt: Q9H6R4
Pockets: 17 · best druggability 0.83

Structure

1 distinct chain · 41% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nucleolar protein 6	protein	1146	41% helix, 15% strand	Q9H6R4

Pockets

17 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	817	0.83	0.85	98	empty
2	949	0.77	0.80	81	empty
3	451	0.73	0.82	40	empty
4	306	0.71	0.85	50	empty
5	120	0.55	0.83	24	empty

Compared structures

7MQA · Cryo-EM structure of the human SSU processome, state post-A1 · an experimental structure of the same protein · chain A against NH, TM-score 0.91
7MQ8 · Cryo-EM structure of the human SSU processome, state pre-A1 · an experimental structure of the same protein · chain A against NH, TM-score 0.91
7MQ9 · Cryo-EM structure of the human SSU processome, state pre-A1* · an experimental structure of the same protein · chain A against NH, TM-score 0.91

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 Q9H6R4
Elsewhere: UniProt Q9H6R4 · AlphaFold DB Q9H6R4

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