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AlphaFold monomer V2.0 prediction for phosphorylated adapter RNA export protein (Q9H814)

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

Accession: Q9H814
Type: protein
Length: 394 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x4d07E6a23DeB6B95bd9b90EcB67368b7e8D3B77e
Molecule: Phosphorylated adapter RNA export protein
UniProt: Q9H814
Pockets: 3 · best druggability 0.39

Structure

1 distinct chain · 42% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphorylated adapter RNA export protein	protein	394	42% helix, 1% strand	Q9H814

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	75	0.39	0.78	12	empty
2	65	0.32	0.75	11	empty
3	50	0.28	0.75	12	empty

Compared structures

2XC7 · Solution Structure of PHAX-RBD in complex with ssRNA · an experimental structure of the same protein · chain A against A, TM-score 0.22
2XC7 · Solution structure of phax-rbd in complex with ssrna · an experimental structure of the same protein · chain A against A, TM-score 0.22
8PNT · Structure of the human nuclear cap-binding complex bound to PHAX and m7G-capped RNA · an experimental structure of the same protein · chain A against C, TM-score 0.05

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 Q9H814
Elsewhere: UniProt Q9H814 · AlphaFold DB Q9H814

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