MolNFT v1 · #17658 · protein

Crystal structure of tRNA-guanine transglycosylase (tgt) from zymomonas mobilis complexed with archaeosine precursor, PREQ0

1P0B · Queuine tRNA-ribosyltransferase: “Crystal structure of tRNA-guanine transglycosylase (tgt) from zymomonas mobilis complexed with archaeosine…”. X-ray diffraction, 2 ligands (PQ0, ZN), 2 pockets (best druggability 0.62). MolNFT v1…

PDB: 1P0B
Type: protein
Length: 369 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: PQ0, ZN
Pockets: 2 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Queuine tRNA-ribosyltransferase (EC 2.4.2.29)	protein	369	46% helix, 19% strand	P28720

Ligands and binding sites

PQ0 · 2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile · 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	235	0.62	0.81	40	PQ0
2	55	0.35	0.79	11	empty

Compared structures

1P0B · Crystal Structure Of tRNA-Guanine Transglycosylase (TGT) From Zymomonas mobilis Complexed… · 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 1P0B · PDBe 1P0B · UniProt P28720

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