Research workbench
Crystal structure of outer surface protein C (ospc)
Analyse Crystal structure of outer surface protein C (ospc) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1F1M
- 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
- Q9AGB1
- Ligands
- ZN
- Pockets
- 3 · best druggability 0.42
Structure
x-ray diffraction · 1 distinct chain · 67% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Outer surface protein C | protein | 162 | 67% helix, 2% strand | Q9AGB1 |
Ligands and binding sites
- ZN · Zinc ion · metal · 6 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 122 | 0.42 | 0.76 | 21 | empty |
| 2 | 96 | 0.41 | 0.77 | 22 | empty |
| 3 | 106 | 0.39 | 0.75 | 17 | empty |
Interfaces
2 interfaces between chains.
- A–B · 2310 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 2267 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 1F1M · Crystal structure of outer surface protein C (ospc) · 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 Q9AGB1
- Elsewhere: RCSB PDB 1F1M · PDBe 1F1M · UniProt Q9AGB1
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