Research workbench
Atomic-resolution crystal structure of borrelia burgdorferi ospa via surface entropy reduction
Analyse Atomic-resolution crystal structure of borrelia burgdorferi ospa via surface… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2G8C
- Type
- protein
- Length
- 246 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Outer surface protein a
- UniProt
- P14013
- Pockets
- 2 · best druggability 0.34
Structure
x-ray diffraction · 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 | P14013 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 84 | 0.34 | 0.74 | 19 | IMD, PG4 |
| 2 | 66 | 0.33 | 0.75 | 16 | PG4 |
Compared structures
- 2G8C · Atomic-resolution crystal structure of Borrelia burgdorferi OspA via surface entropy… · the same entry in another collection · chain O against O, 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 P14013
- Elsewhere: RCSB PDB 2G8C · PDBe 2G8C · UniProt P14013
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.