Research workbench

AlphaFold monomer V2.0 prediction for RAS-related protein rab-9A (P51151)

Analyse AlphaFold monomer V2.0 prediction for RAS-related protein rab-9A (P51151) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: P51151
Type: protein
Length: 201 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x0EA189b2343A464f560b44103f6A3396Da1dA8a9
Molecule: RAS-related protein rab-9A
UniProt: P51151
Pockets: 2 · best druggability 0.47

Structure

1 distinct chain · 36% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	RAS-related protein rab-9A	protein	201	36% helix, 22% strand	P51151

Pockets

2 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	117	0.47	0.79	28	empty
2	92	0.35	0.74	19	empty

Compared structures

7E1T · Crystal structure of Rab9A-GTP-Nde1 · an experimental structure of the same protein · chain A against B, TM-score 0.86
7E1T · Crystal structure of RAB9A-GTP-NDE1 · an experimental structure of the same protein · chain A against B, TM-score 0.86
1WMS · High resolution crystal structure of human RAB9 GTPase: a novel antiviral drug target · an experimental structure of the same protein · chain A against A, TM-score 0.81
1WMS · High resolution crystal structure of human Rab9 GTPase: a novel antiviral drug target · an experimental structure of the same protein · chain A against A, TM-score 0.81

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 P51151
Elsewhere: UniProt P51151 · AlphaFold DB P51151

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