MolNFT v1 · #79498 · protein
X-ray structure of the lov domain from the lov-hk sensory protein from brucella abortus (dark state).
3T50 · Blue-light-activated histidine kinase: “X-ray structure of the lov domain from the lov-hk sensory protein from brucella abortus (dark state).”. X-ray diffraction, 1 ligand (FMN), 3 pockets (best druggability 0.69). MolNFT v1 #79498…
- PDB
- 3T50
- Type
- protein
- Length
- 223 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Blue-light-activated histidine kinase
- EC
- 2.7.13.3
- UniProt
- Q8YC53
- Ligands
- FMN
- Pockets
- 3 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 26% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Blue-light-activated histidine kinase (EC 2.7.13.3) | protein | 115 | 27% helix, 33% strand | Q8YC53 |
| B | Blue-light-activated histidine kinase (EC 2.7.13.3) | protein | 108 | 24% helix, 35% strand | Q8YC53 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 157 | 0.69 | 0.88 | 24 | FMN |
| 2 | 162 | 0.69 | 0.88 | 22 | FMN |
| 3 | 74 | 0.41 | 0.79 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 899 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 3T50 · X-ray structure of the LOV domain from the LOV-HK sensory protein from Brucella abortus… · the same entry in another collection · chain A against A, TM-score 1.00
- Q8YC53 · AlphaFold monomer V2.0 prediction for blue-light-activated histidine kinase (Q8YC53) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 Q8YC53
- Elsewhere: RCSB PDB 3T50 · PDBe 3T50 · UniProt Q8YC53
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