Research workbench
BBE31 from lyme disease agent borrelia (borreliella) burgdorferi playing a vital role in successful colonization of the mammalian host (native data)
Analyse BBE31 from lyme disease agent borrelia (borreliella) burgdorferi playing a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FZE
- Type
- protein
- Length
- 410 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O50725
- Ligands
- GSH, SO4
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 209 | — | O50725 |
| B | — | protein | 201 | — | O50725 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6FZE · BBE31 from Lyme disease agent Borrelia (Borreliella) burgdorferi playing a vital role in… · 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 O50725
- Elsewhere: RCSB PDB 6FZE · PDBe 6FZE · UniProt O50725
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