Research workbench
Crystal structure of thiamin phosphate synthase from mycobacterium tuberculosis
Analyse Crystal structure of thiamin phosphate synthase from mycobacterium tuberculosis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3O63
- Type
- protein
- Length
- 424 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable thiamine-phosphate pyrophosphorylase
- EC
- 2.5.1.3
- UniProt
- P66916
- Ligands
- PO4
- Pockets
- 6 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable thiamine-phosphate pyrophosphorylase (EC 2.5.1.3) | protein | 214 | 44% helix, 16% strand | P66916 |
| B | Probable thiamine-phosphate pyrophosphorylase (EC 2.5.1.3) | protein | 210 | 43% helix, 17% strand | P66916 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 89 | 0.71 | 0.95 | 29 | empty |
| 2 | 377 | 0.62 | 0.78 | 39 | PO4 |
| 3 | 263 | 0.57 | 0.78 | 41 | PO4 |
| 4 | 103 | 0.39 | 0.76 | 19 | empty |
| 5 | 74 | 0.37 | 0.77 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 705 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 3O63 · Crystal Structure of Thiamin Phosphate Synthase from Mycobacterium tuberculosis · 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 P66916
- Elsewhere: RCSB PDB 3O63 · PDBe 3O63 · UniProt P66916
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