Research workbench
Crystal structure of LOV1 domain of PHOTOTROPIN2 from arabidopsis thaliana
Analyse Crystal structure of LOV1 domain of PHOTOTROPIN2 from arabidopsis thaliana in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Z6D
- Type
- protein
- Length
- 225 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phototropin-2
- EC
- 2.7.11.1
- UniProt
- P93025
- Ligands
- FMN
- Pockets
- 3 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 27% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phototropin-2 (EC 2.7.11.1) | protein | 118 | 29% helix, 34% strand | P93025 |
| B | Phototropin-2 (EC 2.7.11.1) | protein | 107 | 25% helix, 37% 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 | 196 | 0.72 | 0.88 | 25 | FMN |
| 2 | 202 | 0.72 | 0.88 | 26 | FMN |
| 3 | 54 | 0.27 | 0.74 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1003 Ų buried · 4 hydrogen bonds · protein-protein
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 2Z6D · PDBe 2Z6D · UniProt P93025
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