MolNFT v1 · #121478 · protein
Crystal structure of apo-PAS1
5HWT · Sensor histidine kinase tods: “Crystal structure of apo-PAS1”. X-ray diffraction, 5 pockets (best druggability 0.74). MolNFT v1 #121478 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5HWT
- Type
- protein
- Length
- 247 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sensor histidine kinase tods
- EC
- 2.7.13.3
- UniProt
- A5W4E3
- Pockets
- 5 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sensor histidine kinase tods (EC 2.7.13.3) | protein | 125 | 38% helix, 37% strand | A5W4E3 |
| B | Sensor histidine kinase tods (EC 2.7.13.3) | protein | 122 | 26% helix, 38% strand | A5W4E3 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 56 | 0.74 | 0.99 | 15 | empty |
| 2 | 50 | 0.73 | 0.99 | 15 | empty |
| 3 | 107 | 0.59 | 0.85 | 20 | empty |
| 4 | 109 | 0.44 | 0.78 | 25 | empty |
| 5 | 128 | 0.43 | 0.76 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 873 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified (engineered).
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 A5W4E3
- Elsewhere: RCSB PDB 5HWT · PDBe 5HWT · UniProt A5W4E3
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