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AlphaFold monomer V2.0 prediction for tRNA (PSEUDOURIDINE(54)-N(1))-methyltransferase (O29206)

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

Accession: O29206
Type: protein
Length: 288 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x22F6EB540e0Df2CeE21099Ba0563dE8C1f0D8763
Molecule: TRNA (PSEUDOURIDINE(54)-N(1))-methyltransferase
UniProt: O29206
Pockets: 2 · best druggability 0.56

Structure

1 distinct chain · 23% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	TRNA (PSEUDOURIDINE(54)-N(1))-methyltransferase	protein	288	23% helix, 18% strand	O29206

Pockets

2 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	109	0.56	0.84	25	empty
2	145	0.48	0.78	22	empty

Compared structures

2QMM · Crystal structure of APC86534.1 (C-terminal domain of NCBI AAB90184.1; Pfam BIG 123.1) · an experimental structure of the same protein · chain A against A, TM-score 0.68
2QMM · Crystal structure of APC86534.1 (C-terminal domain of ncbi AAB90184.1; pfam big 123.1) · an experimental structure of the same protein · chain A against A, TM-score 0.68

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 O29206
Elsewhere: UniProt O29206 · AlphaFold DB O29206

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