MolNFT v1 · #62404 · protein
The crystal structure of the domain of the putative light and redox sensing histidine kinase from haloarcula marismortui
3EEH: “The crystal structure of the domain of the putative light and redox sensing histidine kinase from haloarcula…”. X-ray diffraction, 1 pocket (best druggability 0.74). MolNFT v1 #62404 on GenesisL1: 3D structure, binding sites and…
- 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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