Research workbench
Crystal structure of thiazole kinase mutant (C198S) with ATP and thiazole phosphate.
Analyse Crystal structure of thiazole kinase mutant (C198S) with ATP and thiazole… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ESQ
- Type
- protein
- Length
- 790 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hydroxyethylthiazole kinase
- EC
- 2.7.1.50
- UniProt
- P39593
- Ligands
- ATP, TZP, MG, SO4
- Pockets
- 7 · best druggability 0.79
Structure
x-ray diffraction · 3 distinct chains · 55% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hydroxyethylthiazole kinase (EC 2.7.1.50) | protein | 258 | 55% helix, 15% strand | P39593 |
| B | Hydroxyethylthiazole kinase (EC 2.7.1.50) | protein | 258 | 55% helix, 16% strand | P39593 |
| C | Hydroxyethylthiazole kinase (EC 2.7.1.50) | protein | 274 | 54% helix, 15% strand | P39593 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 3 copies · chains A, B, C
- TZP · 4-methyl-5-hydroxyethylthiazole phosphate · ligand · 3 copies · chains A, B, C
- MG · Magnesium ion · metal · 6 copies · chains A, B, C
- SO4 · Sulfate ion · ion · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 707 | 0.79 | 0.83 | 54 | SO4 |
| 2 | 591 | 0.70 | 0.78 | 44 | MG, ATP, TZP |
| 3 | 539 | 0.69 | 0.79 | 45 | MG, ATP, TZP |
| 4 | 557 | 0.69 | 0.79 | 46 | MG, ATP, TZP |
| 5 | 50 | 0.68 | 0.97 | 27 | empty |
Interfaces
3 interfaces between chains.
- A–B · 970 Ų buried · 19 hydrogen bonds · protein-protein
- B–C · 953 Ų buried · 15 hydrogen bonds · protein-protein
- A–C · 949 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 1ESQ · Crystal structure of thiazole kinase mutant (C198S) with ATP and thiazole phosphate. · the same entry in another collection · chain A against A, TM-score 1.00
- P39593 · AlphaFold monomer V2.0 prediction for hydroxyethylthiazole kinase (P39593) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 P39593
- Elsewhere: RCSB PDB 1ESQ · PDBe 1ESQ · UniProt P39593
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