Research workbench
The crystal structure of the domain of the putative light and redox sensing histidine kinase from haloarcula marismortui
Analyse The crystal structure of the domain of the putative light and redox sensing… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3EEH
- Type
- protein
- Length
- 116 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative light and redox sensing histidine kinase
- EC
- 2.7.13.3
- UniProt
- Q5UZS4
- Pockets
- 1 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative light and redox sensing histidine kinase (EC 2.7.13.3) | protein | 116 | 38% helix, 34% strand | Q5UZS4 |
Ligands and binding sites
- PG5 · 1-methoxy-2-[2-(2-methoxy-ethoxy]-ethane · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 142 | 0.74 | 0.91 | 26 | PG5 |
Compared structures
- 3EEH · The crystal structure of the domain of the putative light and redox sensing histidine… · the same entry in another collection · chain A against A, TM-score 1.00
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 Q5UZS4
- Elsewhere: RCSB PDB 3EEH · PDBe 3EEH · UniProt Q5UZS4
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