Research workbench

AlphaFold monomer V2.0 prediction for spindle assembly abnormal protein 5 (Q20010)

Analyse AlphaFold monomer V2.0 prediction for spindle assembly abnormal protein 5… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: Q20010
Type: protein
Length: 404 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x1620032580Cf2476f2BD828E85045251C289D3d8
Molecule: Spindle assembly abnormal protein 5
UniProt: Q20010
Pockets: 1 · best druggability 0.61

Structure

1 distinct chain · 31% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Spindle assembly abnormal protein 5	protein	404	31% helix, 1% strand	Q20010

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	392	0.61	0.76	28	empty

Compared structures

4YNH · Structure of the C. elegans SAS-5 Implico dimerization domain · an experimental structure of the same protein · chain A against A, TM-score 0.14
4YNH · Structure of the C. elegans sas-5 implico dimerization domain · an experimental structure of the same protein · chain A against A, TM-score 0.14
4YV4 · Structure of the C. elegans sas-5 coiled coil domain · an experimental structure of the same protein · chain A against C, TM-score 0.14
4YV4 · Structure of the C. elegans SAS-5 coiled coil domain · an experimental structure of the same protein · chain A against C, TM-score 0.14

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 Q20010
Elsewhere: UniProt Q20010 · AlphaFold DB Q20010

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