MolNFT v1 · #2670 · protein
Crystal structure of native thiazole kinase in the monoclinic form
1C3Q · Hydroxyethylthiazole kinase: “Crystal structure of native thiazole kinase in the monoclinic form”. X-ray diffraction, 2 ligands (TZE, CL), 10 pockets (best druggability 0.81). MolNFT v1 #2670 on GenesisL1: 3D structure, binding…
- PDB
- 1C3Q
- Type
- protein
- Length
- 852 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
- TZE, CL
- Pockets
- 10 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Hydroxyethylthiazole kinase (EC 2.7.1.50) | protein | 284 | 51% helix, 14% strand | P39593 |
Ligands and binding sites
- TZE · 2-(4-methyl-thiazol-5-yl)-ethanol · ligand · 3 copies · chains A, C, B
- CL · Chloride ion · ion · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 817 | 0.81 | 0.84 | 58 | CL |
| 2 | 588 | 0.70 | 0.79 | 45 | TZE |
| 3 | 632 | 0.70 | 0.78 | 47 | TZE |
| 4 | 51 | 0.70 | 0.98 | 18 | empty |
| 5 | 568 | 0.67 | 0.77 | 49 | TZE |
Interfaces
3 interfaces between chains.
- A–C · 968 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 959 Ų buried · 15 hydrogen bonds · protein-protein
- B–C · 885 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 1C3Q · Crystal structure of native thiazole kinase in the monoclinic form · 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 A against A, TM-score 0.93
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 1C3Q · PDBe 1C3Q · UniProt P39593
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