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AlphaFold monomer V2.0 prediction for xk-related protein 8 (Q9H6D3)

Analyse AlphaFold monomer V2.0 prediction for xk-related protein 8 (Q9H6D3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: Q9H6D3
Type: protein
Length: 395 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x7012c0b45c68a2c067644b9d3e5DDa06892c6957
Molecule: Xk-related protein 8
UniProt: Q9H6D3
Pockets: 7 · best druggability 0.75

Structure

1 distinct chain · 74% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Xk-related protein 8	protein	395	74% helix, 0% strand	Q9H6D3

Pockets

7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	440	0.75	0.84	57	empty
2	392	0.68	0.80	39	empty
3	261	0.66	0.82	34	empty
4	313	0.63	0.79	33	empty
5	83	0.44	0.80	19	empty

Compared structures

8XEJ · Cryo-EM structure of human XKR8-basigin complex in lipid nanodisc · an experimental structure of the same protein · chain A against X, TM-score 0.86
7DCE · Cryo-EM structure of human XKR8-basigin complex bound to Fab fragment · an experimental structure of the same protein · chain A against X, TM-score 0.85
7DCE · Cryo-EM structure of human XKR8-basigin complex bound to Fab fragment · an experimental structure of the same protein · chain A against X, TM-score 0.83

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 Q9H6D3
Elsewhere: UniProt Q9H6D3 · AlphaFold DB Q9H6D3

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