MolNFT v1 · #121480 · protein
Crystal structure of PAS1 complexed with toluene
5HWV · Sensor histidine kinase tods: “Crystal structure of PAS1 complexed with toluene”. X-ray diffraction, 1 ligand (MBN), 4 pockets (best druggability 0.73). MolNFT v1 #121480 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5HWV
- Type
- protein
- Length
- 249 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
- Ligands
- MBN
- Pockets
- 4 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sensor histidine kinase tods (EC 2.7.13.3) | protein | 124 | 40% helix, 37% strand | A5W4E3 |
| B | Sensor histidine kinase tods (EC 2.7.13.3) | protein | 125 | 37% helix, 37% strand | A5W4E3 |
Ligands and binding sites
- MBN · Toluene · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 51 | 0.73 | 0.99 | 16 | MBN |
| 2 | 162 | 0.57 | 0.82 | 24 | empty |
| 3 | 120 | 0.46 | 0.78 | 21 | empty |
| 4 | 53 | 0.27 | 0.74 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 733 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 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 5HWV · PDBe 5HWV · UniProt A5W4E3
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