Research workbench
Borrelia burgdorferi OspA via surface entropy reduction (form3)
Analyse Borrelia burgdorferi OspA via surface entropy reduction (form3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6J6C
- Type
- protein
- Length
- 246 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.6
- Source
- Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
- Molecule
- Outer surface protein A
- UniProt
- P0CL66
- Pockets
- 2 · best druggability 0.30
Structure
x-ray diffraction · resolution 1.6 · 1 distinct chain · 3% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| O | Outer surface protein A | protein | 246 | 3% helix, 54% strand | P0CL66 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 65 | 0.30 | 0.74 | 17 | empty |
| 2 | 70 | 0.29 | 0.73 | 17 | empty |
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 P0CL66
- Elsewhere: RCSB PDB 6J6C · PDBe 6J6C · UniProt P0CL66
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