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Crystal structure of tRNA-guanine transglycosylase (tgt) from zymomonas mobilis in complex with 6-amino-3,7-dihydro-IMIDAZO[4,5- G]QUINAZOLIN-8-one

Analyse Crystal structure of tRNA-guanine transglycosylase (tgt) from zymomonas mobilis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2BBF
Type: protein
Length: 367 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: TRNA guanine transglycosylase
EC: 2.4.2.29
Ligands: 344, ZN
Pockets: 2 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	TRNA guanine transglycosylase (EC 2.4.2.29)	protein	367	44% helix, 19% strand	—

Ligands and binding sites

344 · 6-amino-3,7-dihydro-imidazo[4,5-g]quinazolin-8-one · ligand · chains A
ZN · Zinc ion · metal · 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	270	0.62	0.81	45	344
2	70	0.36	0.78	17	empty

Compared structures

2BBF · Crystal structure of tRNA-guanine transglycosylase (TGT) from Zymomonas mobilis in… · 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
Elsewhere: RCSB PDB 2BBF · PDBe 2BBF

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