Research workbench
Crystal structure of miniSOG at 1.17A resolution
Analyse Crystal structure of miniSOG at 1.17A resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6GPU
- Type
- protein
- Length
- 115 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.17
- Source
- Arabidopsis thaliana
- Molecule
- Phototropin-2
- EC
- 2.7.11.1
- UniProt
- P93025
- Ligands
- FMN, MG, CO, CL
- Pockets
- 1 · best druggability 0.70
Structure
x-ray diffraction · resolution 1.17 · 1 distinct chain · 27% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phototropin-2 (EC 2.7.11.1) | protein | 115 | 27% helix, 34% strand | P93025 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · chains A
- MG · Magnesium ion · metal · chains A
- CO · Cobalt (II) ion · metal · chains A
- CL · Chloride ion · ion · chains A
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 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 | 186 | 0.70 | 0.88 | 25 | FMN, CL |
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 6GPU · PDBe 6GPU · UniProt P93025
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