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AlphaFold monomer V2.0 prediction for ribonuclease 7 (Q9H1E1)

Analyse AlphaFold monomer V2.0 prediction for ribonuclease 7 (Q9H1E1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: Q9H1E1
Type: protein
Length: 156 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0xEa58c7534E5701aA8370E0fAEb19b7e14653e69c
Molecule: Ribonuclease 7
UniProt: Q9H1E1
Pockets: 1 · best druggability 0.42

Structure

1 distinct chain · 24% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ribonuclease 7	protein	156	24% helix, 28% strand	Q9H1E1

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	143	0.42	0.75	20	empty

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

2HKY · NMR solution structure of human RNase 7 · an experimental structure of the same protein · chain A against A, TM-score 0.70
2HKY · NMR solution structure of human RNase 7 · an experimental structure of the same protein · chain A against A, TM-score 0.70

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 Q9H1E1
Elsewhere: UniProt Q9H1E1 · AlphaFold DB Q9H1E1

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