Research workbench
Outer surface protein C (ospc) of borrelia burgdorferi strain B31
Analyse Outer surface protein C (ospc) of borrelia burgdorferi strain B31 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GGQ
- Type
- protein
- Length
- 648 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Outer surface protein C
- UniProt
- Q07337
- Ligands
- MG
- Pockets
- 4 · best druggability 0.38
Structure
x-ray diffraction · 2 distinct chains · 70% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Outer surface protein C | protein | 162 | 71% helix, 5% strand | Q07337 |
| B, D | Outer surface protein C | protein | 162 | 69% helix, 5% strand | Q07337 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 68 | 0.38 | 0.78 | 17 | empty |
| 2 | 67 | 0.34 | 0.76 | 19 | empty |
| 3 | 55 | 0.30 | 0.75 | 18 | empty |
| 4 | 79 | 0.29 | 0.73 | 22 | empty |
Interfaces
3 interfaces between chains.
- A–B · 2144 Ų buried · 11 hydrogen bonds · protein-protein
- C–D · 2137 Ų buried · 11 hydrogen bonds · protein-protein
- A–C · 169 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1GGQ · Outer surface protein C (ospc) of borrelia burgdorferi strain B31 · the same entry in another collection · chain A against A, TM-score 1.00
- Q07337 · AlphaFold monomer V2.0 prediction for outer surface protein C (Q07337) · a predicted model of the same protein · chain B against A, TM-score 0.97
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 Q07337
- Elsewhere: RCSB PDB 1GGQ · PDBe 1GGQ · UniProt Q07337
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