Research workbench
Crystal structure of iLOV-I486z(2LT) at pH 9.0
Analyse Crystal structure of iLOV-I486z(2LT) at pH 9.0 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4NXG
- Type
- protein
- Length
- 207 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.09
- Source
- Arabidopsis thaliana
- Molecule
- Phototropin-2
- EC
- 2.7.11.1
- UniProt
- P93025
- Ligands
- FMN
- Pockets
- 3 · best druggability 0.68
Structure
x-ray diffraction · resolution 2.09 · 2 distinct chains · 27% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phototropin-2 (EC 2.7.11.1) | protein | 103 | 27% helix, 36% strand | P93025 |
| B | Phototropin-2 (EC 2.7.11.1) | protein | 104 | 27% helix, 32% strand | P93025 |
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 | 175 | 0.68 | 0.87 | 24 | FMN |
| 2 | 165 | 0.67 | 0.87 | 22 | FMN |
| 3 | 56 | 0.37 | 0.79 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 808 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (nonstandard).
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 P93025
- Elsewhere: RCSB PDB 4NXG · PDBe 4NXG · UniProt P93025
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