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TRNA-guanine transglycosylase (tgt) in co-crystallized complex with 6- amino-4-[2-(4-METHOXYPHENYL)ETHYL]-1,7-dihydro-8H-IMIDAZO[4,5- G]QUINAZOLIN-8-one

Analyse TRNA-guanine transglycosylase (tgt) in co-crystallized complex with 6… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5I06
Type: protein
Length: 355 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Queuine tRNA-ribosyltransferase
EC: 2.4.2.29
UniProt: P28720
Ligands: E89, ZN
Pockets: 3 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Queuine tRNA-ribosyltransferase (EC 2.4.2.29)	protein	355	46% helix, 16% strand	P28720

Ligands and binding sites

E89 · 6-amino-4-[2-(4-methoxyphenyl)ethyl]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one · ligand · chains A
ZN · Zinc ion · metal · chains A
GOL · Glycerol · additive · 3 copies · chains A
EDO · 1,2-ethanediol · additive · chains A
PGE · Triethylene glycol · additive · chains A

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

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	254	0.61	0.80	38	E89
2	53	0.35	0.79	18	GOL
3	54	0.31	0.76	12	empty

Compared structures

5I06 · tRNA-guanine Transglycosylase (TGT) in co-crystallized complex with… · the same entry in another collection · chain A against A, TM-score 1.00

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 P28720
Elsewhere: RCSB PDB 5I06 · PDBe 5I06 · UniProt P28720

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