Research workbench
Cryogenic temperature structure of the ground state of ATPHOT2LOV2 recorded after an accumulated dose of 2.68 mgy
Analyse Cryogenic temperature structure of the ground state of ATPHOT2LOV2 recorded… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6QQH
- Type
- protein
- Length
- 117 residues
- Chains
- 1
- 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
- 1 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phototropin-2 (EC 2.7.11.1) | protein | 117 | 27% helix, 32% strand | P93025 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 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 | 172 | 0.72 | 0.89 | 24 | FMN |
Compared structures
- 6QQH · Cryogenic temperature structure of the ground state of AtPhot2LOV2 recorded after an… · the same entry in another collection · chain A against A, TM-score 1.00
- P93025 · AlphaFold monomer V2.0 prediction for phototropin-2 (P93025) · a predicted model of the same protein · chain A against A, TM-score 0.92
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 6QQH · PDBe 6QQH · UniProt P93025
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