Research workbench
2.5A X-ray structure of engineered ospa protein
Analyse 2.5A X-ray structure of engineered ospa protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2AF5
- Type
- protein
- Length
- 292 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Engineered outer surface protein a (ospa) with the inserted two beta-hairpins
- UniProt
- P14013
- Pockets
- 2 · best druggability 0.44
Structure
x-ray diffraction · 1 distinct chain · 2% helix, 55% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Engineered outer surface protein a (ospa) with the inserted two beta-hairpins | protein | 292 | 2% helix, 55% strand | P14013 |
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 | 160 | 0.44 | 0.75 | 29 | empty |
| 2 | 61 | 0.32 | 0.76 | 15 | empty |
Compared structures
- 2AF5 · 2.5A X-ray Structure of Engineered OspA protein · 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 P14013
- Elsewhere: RCSB PDB 2AF5 · PDBe 2AF5 · UniProt P14013
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