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AlphaFold monomer V2.0 prediction for zinc METALLOPROTEINASE/DISINTEGRIN (Q805F6)

Analyse AlphaFold monomer V2.0 prediction for zinc METALLOPROTEINASE/DISINTEGRIN… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: Q805F6
Type: protein
Length: 483 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x2BfFDbEAFa18c028B2FfB28D507b26e3fD3E6cf3
Molecule: Zinc METALLOPROTEINASE/DISINTEGRIN
UniProt: Q805F6
Pockets: 7 · best druggability 0.68

Structure

1 distinct chain · 17% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Zinc METALLOPROTEINASE/DISINTEGRIN	protein	483	17% helix, 25% strand	Q805F6

Pockets

7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	343	0.68	0.82	38	empty
2	177	0.59	0.82	32	empty
3	249	0.53	0.76	36	empty
4	95	0.49	0.81	23	empty
5	89	0.47	0.81	22	empty

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

3C05 · Crystal structure of Acostatin from Agkistrodon Contortrix Contortrix · an experimental structure of the same protein · chain A against B, TM-score 0.12
3C05 · Crystal structure of acostatin from agkistrodon contortrix contortrix · an experimental structure of the same protein · chain A against B, TM-score 0.12

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 Q805F6
Elsewhere: UniProt Q805F6 · AlphaFold DB Q805F6

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