Research workbench

AlphaFold monomer V2.0 prediction for tryptophan--tRNA ligase (Q9KNV7)

Analyse AlphaFold monomer V2.0 prediction for tryptophan--tRNA ligase (Q9KNV7) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: Q9KNV7
Type: protein
Length: 338 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0xbD251E094c0E2A0f68B35A89062EA0CDfcddA477
Molecule: Tryptophan--tRNA ligase
UniProt: Q9KNV7
Pockets: 3 · best druggability 0.75

Structure

1 distinct chain · 55% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tryptophan--tRNA ligase	protein	338	55% helix, 9% strand	Q9KNV7

Pockets

3 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	726	0.75	0.80	61	empty
2	126	0.43	0.76	23	empty
3	58	0.28	0.74	14	empty

Compared structures

3SZ3 · Crystal structure of tryptophanyl-tRNA synthetase from vibrio cholerae with an endogenous… · an experimental structure of the same protein · chain A against A, TM-score 0.97
3SZ3 · Crystal structure of Tryptophanyl-tRNA synthetase from Vibrio cholerae with an endogenous… · an experimental structure of the same protein · chain A against A, TM-score 0.97

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 Q9KNV7
Elsewhere: UniProt Q9KNV7 · AlphaFold DB Q9KNV7

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