Research workbench

Crystal structure of human tRNA-dihydrouridine (20) synthase dsrbd F359A mutant

Analyse Crystal structure of human tRNA-dihydrouridine (20) synthase dsrbd F359A mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6EI8
Type: protein
Length: 97 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: TRNA-DIHYDROURIDINE(20) synthase [NAD(P)+]-like
EC: 1.3.1.-
UniProt: Q9NX74
Ligands: SO4
Pockets: 1 · best druggability 0.29

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	TRNA-DIHYDROURIDINE(20) synthase [NAD(P)+]-like (EC 1.3.1.-)	protein	97	29% helix, 26% strand	Q9NX74

Ligands and binding sites

SO4 · Sulfate ion · ion · 3 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	61	0.29	0.74	15	empty

Compared structures

6EI8 · Crystal structure of human tRNA-dihydrouridine (20) synthase dsRBD F359A mutant · the same entry in another collection · chain A against A, TM-score 1.00
Q9NX74 · AlphaFold monomer V2.0 prediction for tRNA-DIHYDROURIDINE(20) synthase [NAD(P)+]-like… · a predicted model of the same protein · chain A against A, TM-score 0.88

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 Q9NX74
Elsewhere: RCSB PDB 6EI8 · PDBe 6EI8 · UniProt Q9NX74

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.