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AlphaFold monomer V2.0 prediction for non-structural maintenance of chromosomes element 3 homolog (Q96MG7)

Analyse AlphaFold monomer V2.0 prediction for non-structural maintenance of chromosomes… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: Q96MG7
Type: protein
Length: 304 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x5e58272ea25a05e06901A2eAe9f63939b344e0c6
Molecule: Non-structural maintenance of chromosomes element 3 homolog
UniProt: Q96MG7
Pockets: 1 · best druggability 0.65

Structure

1 distinct chain · 39% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Non-structural maintenance of chromosomes element 3 homolog	protein	304	39% helix, 9% strand	Q96MG7

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	456	0.65	0.78	44	empty

Compared structures

5HVQ · Alternative model of the mage-G1 nse-1 complex · an experimental structure of the same protein · chain A against D, TM-score 0.36
5WY5 · Crystal structure of MAGEG1 and NSE1 complex · an experimental structure of the same protein · chain A against B, TM-score 0.34
5WY5 · Crystal structure of MAGEG1 and NSE1 complex · an experimental structure of the same protein · chain A against B, TM-score 0.34

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 Q96MG7
Elsewhere: UniProt Q96MG7 · AlphaFold DB Q96MG7

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