Research workbench

AlphaFold monomer V2.0 prediction for RNA-binding protein nova-1 (P51513)

Analyse AlphaFold monomer V2.0 prediction for RNA-binding protein nova-1 (P51513) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: P51513
Type: protein
Length: 507 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0xc785fb0860a7632894499957946e549eec043885
Molecule: RNA-binding protein nova-1
UniProt: P51513
Pockets: 6 · best druggability 0.55

Structure

1 distinct chain · 36% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	RNA-binding protein nova-1	protein	507	36% helix, 13% strand	P51513

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	347	0.55	0.74	37	empty
2	273	0.49	0.73	26	empty
3	71	0.45	0.82	19	empty
4	57	0.29	0.75	17	empty
5	62	0.29	0.74	17	empty

Compared structures

2ANR · Crystal structure (II) of nova-1 KH1/KH2 domain tandem with 25NT RNA hairpin · an experimental structure of the same protein · chain A against A, TM-score 0.30
1DT4 · Crystal structure of nova-1 KH3 K-homology RNA-binding domain · an experimental structure of the same protein · chain A against A, TM-score 0.14
1DT4 · Crystal structure of nova-1 KH3 K-homology RNA-binding domain · an experimental structure of the same protein · chain A against A, TM-score 0.14

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 P51513
Elsewhere: UniProt P51513 · AlphaFold DB P51513

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