Research workbench
Crystal structure of bacillus subtilis thiamin phosphate synthase complexed with a carboxylated thiazole phosphate
Analyse Crystal structure of bacillus subtilis thiamin phosphate synthase complexed… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3O15
- Type
- protein
- Length
- 219 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thiamine-phosphate pyrophosphorylase
- EC
- 2.5.1.3
- UniProt
- P39594
- Ligands
- 3NM, IFP, POP
- Pockets
- 1 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thiamine-phosphate pyrophosphorylase (EC 2.5.1.3) | protein | 219 | 44% helix, 16% strand | P39594 |
Ligands and binding sites
- 3NM · 4-methyl-5-[2-(phosphonooxy)ethyl]-1,3-thiazole-2-carboxylic acid · ligand · chains A
- IFP · 2-trifluoromethyl-5-methylene-5H-pyrimidin-4-ylideneamine · ligand · chains A
- POP · Pyrophosphate 2- · ligand · chains A
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 | 218 | 0.72 | 0.88 | 37 | 3NM, IFP, POP |
Compared structures
- 3O15 · Crystal Structure of Bacillus subtilis Thiamin Phosphate Synthase Complexed with a… · the same entry in another collection · chain A against A, TM-score 1.00
- P39594 · AlphaFold monomer V2.0 prediction for thiamine-phosphate synthase (P39594) · a predicted model of the same protein · 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 P39594
- Elsewhere: RCSB PDB 3O15 · PDBe 3O15 · UniProt P39594
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