Research workbench
Crystal structure of light activated transcription factor EL222 from erythrobacter litoralis
Analyse Crystal structure of light activated transcription factor EL222 from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3P7N
- Type
- protein
- Length
- 382 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sensor histidine kinase
- UniProt
- Q2NB98
- Ligands
- FMN
- Pockets
- 5 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Sensor histidine kinase | protein | 191 | 47% helix, 20% strand | Q2NB98 |
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
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 450 | 0.80 | 0.88 | 45 | FMN |
| 2 | 236 | 0.69 | 0.85 | 26 | FMN |
| 3 | 101 | 0.62 | 0.88 | 19 | empty |
| 4 | 244 | 0.60 | 0.80 | 28 | empty |
| 5 | 107 | 0.36 | 0.74 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 491 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 3P7N · Crystal structure of light activated transcription factor El222 from Erythrobacter… · the same entry in another collection · chain A against A, TM-score 1.00
- Q2NB98 · AlphaFold monomer V2.0 prediction for light-activated DNA-binding protein EL222 (Q2NB98) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 Q2NB98
- Elsewhere: RCSB PDB 3P7N · PDBe 3P7N · UniProt Q2NB98
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