Research workbench
Crystal structure of tgt in complex with 2,6-diamino-3H-quinazolin-4- one
Analyse Crystal structure of tgt in complex with 2,6-diamino-3H-quinazolin-4- one in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Q4W
- Type
- protein
- Length
- 364 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
- DQU, ZN
- Pockets
- 4 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Queuine tRNA-ribosyltransferase (EC 2.4.2.29) | protein | 364 | 45% helix, 18% strand | P28720 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 202 | 0.61 | 0.82 | 30 | DQU |
| 2 | 209 | 0.58 | 0.79 | 18 | empty |
| 3 | 59 | 0.43 | 0.82 | 19 | empty |
| 4 | 69 | 0.35 | 0.77 | 18 | empty |
Compared structures
- 1Q4W · Crystal structure of tgt in complex with 2,6-diamino-3H-quinazolin-4-one · 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 1Q4W · PDBe 1Q4W · UniProt P28720
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