Research workbench

AlphaFold monomer V2.0 prediction for selenocysteine lyase (Q96I15)

Analyse AlphaFold monomer V2.0 prediction for selenocysteine lyase (Q96I15) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: Q96I15
Type: protein
Length: 445 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x0EA189b2343A464f560b44103f6A3396Da1dA8a9
Molecule: Selenocysteine lyase
UniProt: Q96I15
Pockets: 6 · best druggability 0.55

Structure

1 distinct chain · 40% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Selenocysteine lyase	protein	445	40% helix, 13% strand	Q96I15

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	193	0.55	0.79	41	empty
2	116	0.54	0.83	24	empty
3	89	0.41	0.78	23	empty
4	61	0.40	0.80	15	empty
5	59	0.30	0.75	16	empty

Compared structures

3GZC · Structure of human selenocysteine lyase · an experimental structure of the same protein · chain A against A, TM-score 0.90
3GZC · Structure of human selenocysteine lyase · an experimental structure of the same protein · chain A against A, TM-score 0.90
3GZD · Human selenocysteine lyase, P1 crystal form · an experimental structure of the same protein · chain A against A, TM-score 0.89
3GZD · Human selenocysteine lyase, P1 crystal form · an experimental structure of the same protein · chain A against A, TM-score 0.89

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 Q96I15
Elsewhere: UniProt Q96I15 · AlphaFold DB Q96I15

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