Research workbench
Thiopurine S-methyltransferase
Analyse Thiopurine S-methyltransferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3BGD
- Type
- protein
- Length
- 464 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thiopurine S-methyltransferase
- EC
- 2.1.1.67
- UniProt
- O55060
- Ligands
- PM6, SAH
- Pockets
- 4 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Thiopurine S-methyltransferase (EC 2.1.1.67) | protein | 232 | 30% helix, 26% strand | O55060 |
Ligands and binding sites
- PM6 · 9H-purine-6-thiol · ligand · 4 copies · chains A, B
- SAH · S-adenosyl-L-homocysteine · ligand · 2 copies · chains A, B
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 | 608 | 0.80 | 0.85 | 82 | SAH, PM6 |
| 2 | 334 | 0.79 | 0.89 | 54 | SAH, PM6 |
| 3 | 56 | 0.38 | 0.80 | 12 | empty |
| 4 | 64 | 0.33 | 0.76 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 208 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
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 O55060
- Elsewhere: RCSB PDB 3BGD · PDBe 3BGD · UniProt O55060
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