Research workbench
Crystal structure of outer surface protein C (ospc) from borrelia burgdorferi
Analyse Crystal structure of outer surface protein C (ospc) from borrelia burgdorferi in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7BML
- Type
- protein
- Length
- 640 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Outer surface protein C
- UniProt
- Q44977
- Pockets
- 2 · best druggability 0.82
Structure
x-ray diffraction · 4 distinct chains · 69% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Outer surface protein C | protein | 161 | 69% helix, 4% strand | Q44977 |
| B | Outer surface protein C | protein | 156 | 70% helix, 4% strand | Q44977 |
| C | Outer surface protein C | protein | 159 | 71% helix, 4% strand | Q44977 |
| D | Outer surface protein C | protein | 164 | 67% helix, 4% strand | Q44977 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1028 | 0.82 | 0.83 | 90 | empty |
| 2 | 387 | 0.63 | 0.78 | 61 | empty |
Interfaces
5 interfaces between chains.
- C–D · 2167 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 2113 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 694 Ų buried · 9 hydrogen bonds · protein-protein
- A–D · 316 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 285 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 7BML · Crystal structure of outer surface protein C (OspC) from Borrelia burgdorferi · 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 Q44977
- Elsewhere: RCSB PDB 7BML · PDBe 7BML · UniProt Q44977
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