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TRNA guanine transglycosylase (tgt) in co-crystallized complex with 2- (methylamino)-1H-BENZO[D]IMIDAZOLE-5-carbohydrazide

Analyse TRNA guanine transglycosylase (tgt) in co-crystallized complex with 2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5J9N
Type: protein
Length: 368 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: 6H9, ZN
Pockets: 2 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Queuine tRNA-ribosyltransferase (EC 2.4.2.29)	protein	368	46% helix, 18% strand	P28720

Ligands and binding sites

6H9 · 2-(methylamino)-1H-benzimidazole-5-carbohydrazide · ligand · chains A
ZN · Zinc ion · metal · chains A
GOL · Glycerol · additive · 3 copies · chains A

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

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	315	0.67	0.82	49	6H9
2	57	0.35	0.78	15	empty

Compared structures

5J9N · 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 5J9N · PDBe 5J9N · UniProt P28720

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