Research workbench
The complement inhibitory domain of B. burgdorferi BBK32.
Analyse The complement inhibitory domain of B. burgdorferi BBK32. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6N1L
- Type
- protein
- Length
- 141 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.722
- Source
- Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
- Molecule
- Fibronectin-binding protein BBK32
- UniProt
- O50835
Structure
x-ray diffraction · resolution 1.722 · 1 distinct chain · 85% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fibronectin-binding protein BBK32 | protein | 141 | 85% helix, 0% strand | O50835 |
Compared structures
- 6N1L · The complement inhibitory domain of B. burgdorferi BBK32. · 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 O50835
- Elsewhere: RCSB PDB 6N1L · PDBe 6N1L · UniProt O50835
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.