Research workbench
protein B
Analyse protein B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6OOP
- Type
- protein
- Length
- 392 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.8
- Source
- Escherichia coli
- Molecule
- Multidrug transporter MdfA
- UniProt
- A0A1E5MBX7
- Ligands
- KHJ, PR
- Pockets
- 1 · best druggability 0.80
Structure
x-ray diffraction · resolution 2.8 · 1 distinct chain · 86% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Multidrug transporter MdfA | protein | 392 | 86% helix, 0% strand | A0A1E5MBX7 |
Ligands and binding sites
- KHJ · 1,1'-dimethyl-4,4'-bipyridin-1-ium · ligand · chains A
- PR · Praseodymium ion · metal · 2 copies · 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 | 1195 | 0.80 | 0.82 | 74 | KHJ |
Compared structures
- 6OOP · PROTEIN B · 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
- Every structure of UniProt A0A1E5MBX7
- Elsewhere: RCSB PDB 6OOP · PDBe 6OOP · UniProt A0A1E5MBX7
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