Research workbench
Crystal structure of tgt in complex with 2-amino-8-methylquinazolin- 4(3H)-one
Analyse Crystal structure of tgt in complex with 2-amino-8-methylquinazolin- 4(3H)-one in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1S38
- Type
- protein
- Length
- 364 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- TRNA guanine transglycosylase
- EC
- 2.4.2.29
- UniProt
- P28720
- Ligands
- MAQ, ZN
- Pockets
- 1 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TRNA guanine transglycosylase (EC 2.4.2.29) | protein | 364 | 46% helix, 18% strand | P28720 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 244 | 0.59 | 0.80 | 38 | MAQ |
Compared structures
- 1S38 · Crystal structure of tgt in complex with 2-amino-8-methylquinazolin-4(3H)-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 1S38 · PDBe 1S38 · UniProt P28720
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