Research workbench
Structure of A3_bGFPD, an artificial bi-domain protein based on two different alphaRep domains : A3 and a GFP binding domain (bGFPD)
Analyse Structure of A3_bGFPD, an artificial bi-domain protein based on two different… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FSQ
- Type
- protein
- Length
- 368 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.79
- Source
- synthetic construct
- Molecule
- alphaRep A3_bGFPD
- Ligands
- NA
- Pockets
- 3 · best druggability 0.55
Structure
x-ray diffraction · resolution 2.79 · 1 distinct chain · 78% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | alphaRep A3_bGFPD | protein | 368 | 78% helix, 0% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 155 | 0.55 | 0.81 | 37 | empty |
| 2 | 144 | 0.50 | 0.78 | 22 | empty |
| 3 | 153 | 0.45 | 0.76 | 20 | empty |
Compared structures
- 6FSQ · Structure of A3_BGFPD, an artificial bi-domain protein based on two different alpharep… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 6FSQ · PDBe 6FSQ
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