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Crystal structure of the tRNA pseudouridine synthase trua from thermus thermophilus HB8

Analyse Crystal structure of the tRNA pseudouridine synthase trua from thermus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1VS3
Type: protein
Length: 498 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: TRNA pseudouridine synthase a
EC: 5.4.99.12
UniProt: Q5SHU9
Pockets: 4 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	TRNA pseudouridine synthase a (EC 5.4.99.12)	protein	249	29% helix, 32% strand	Q5SHU9

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	495	0.70	0.80	58	empty
2	196	0.62	0.83	32	empty
3	208	0.58	0.80	32	empty
4	64	0.29	0.74	14	empty

Interfaces

1 interface between chains.

A–B · 1223 Å² buried · 25 hydrogen bonds · protein-protein

Compared structures

1VS3 · Crystal Structure of the tRNA Pseudouridine Synthase TruA From Thermus thermophilus HB8 · the same entry in another collection · chain A against A, TM-score 1.00
Q5SHU9 · AlphaFold monomer V2.0 prediction for tRNA pseudouridine synthase a (Q5SHU9) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q5SHU9
Elsewhere: RCSB PDB 1VS3 · PDBe 1VS3 · UniProt Q5SHU9

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