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AlphaFold monomer V2.0 prediction for transmembrane channel-like protein 1 (Q8R4P5)

Analyse AlphaFold monomer V2.0 prediction for transmembrane channel-like protein 1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: Q8R4P5
Type: protein
Length: 757 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0xb3c0C983Fc44934AC589D7131C08a72544EBB92E
Molecule: Transmembrane channel-like protein 1
UniProt: Q8R4P5
Pockets: 8 · best druggability 0.78

Structure

1 distinct chain · 70% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transmembrane channel-like protein 1	protein	757	70% helix, 1% strand	Q8R4P5

Pockets

8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	754	0.78	0.82	61	empty
2	618	0.71	0.79	58	empty
3	78	0.67	0.93	18	empty
4	204	0.63	0.82	27	empty
5	281	0.55	0.76	42	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

6WUD · Human calcium and integrin binding protein 3 bound to TMC1 residues 303-347 · an experimental structure of the same protein · chain A against B, TM-score 0.06
6WUD · Human Calcium and Integrin Binding Protein 3 Bound to TMC1 Residues 303-347 · an experimental structure of the same protein · chain A against B, TM-score 0.06

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 Q8R4P5
Elsewhere: UniProt Q8R4P5 · AlphaFold DB Q8R4P5

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