Research workbench
Clostridium botulinum hemagglutinin
Analyse Clostridium botulinum hemagglutinin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WIN
- Type
- protein
- Length
- 1,299 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q33CP8, Q45841, Q33CP6
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D | — | protein | 167 | — | Q33CP8 |
| E | — | protein | 419 | — | Q33CP8 |
| C | — | protein | 141 | — | Q45841 |
| A, B | — | protein | 286 | — | Q33CP6 |
Compared structures
- 3WIN · Clostridium botulinum Hemagglutinin · the same entry in another collection · chain D against D, 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 Q33CP8
- Every structure of UniProt Q45841
- Every structure of UniProt Q33CP6
- Elsewhere: RCSB PDB 3WIN · PDBe 3WIN · UniProt Q33CP8 · UniProt Q45841 · UniProt Q33CP6
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