Research workbench
Crystal structure of PAS1 complexed with 1,2,4-tmb
Analyse Crystal structure of PAS1 complexed with 1,2,4-tmb in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5HWW
- Type
- protein
- Length
- 242 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
- XBZ
- Pockets
- 4 · best druggability 0.56
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sensor histidine kinase tods (EC 2.7.13.3) | protein | 128 | 37% helix, 36% strand | A5W4E3 |
| B | Sensor histidine kinase tods (EC 2.7.13.3) | protein | 114 | 28% helix, 40% strand | A5W4E3 |
Ligands and binding sites
- XBZ · 1,2,4-trimethylbenzene · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 125 | 0.56 | 0.83 | 26 | empty |
| 2 | 81 | 0.39 | 0.78 | 16 | empty |
| 3 | 85 | 0.39 | 0.77 | 16 | empty |
| 4 | 74 | 0.38 | 0.78 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 811 Ų buried · 5 hydrogen bonds · protein-protein
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 5HWW · PDBe 5HWW · UniProt A5W4E3
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