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 v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fibronectin-binding protein BBK32
- UniProt
- O50835
Structure
x-ray diffraction · 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
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