Research workbench
Structural basis for the unfolding of anthrax lethal factor by protective antigen oligomers
Analyse Structural basis for the unfolding of anthrax lethal factor by protective… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3KWV
- Type
- protein
- Length
- 2,551 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P13423, P15917
Structure
x-ray diffraction · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 527 | — | P13423 |
| B | — | protein | 526 | — | P13423 |
| C, F | — | protein | 222 | — | P15917 |
| D | — | protein | 526 | — | P13423 |
| E | — | protein | 528 | — | P13423 |
Compared structures
- 3KWV · Structural basis for the unfolding of anthrax lethal factor by protective antigen… · the same entry in another collection · chain F against F, TM-score 1.00
- P13423 · AlphaFold monomer V2.0 prediction for protective antigen (P13423) · a predicted model of the same protein · chain E against A, TM-score 0.98
- P15917 · AlphaFold monomer V2.0 prediction for lethal factor (P15917) · a predicted model of the same protein · chain C against A, TM-score 0.87
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 P13423
- Every structure of UniProt P15917
- Elsewhere: RCSB PDB 3KWV · PDBe 3KWV · UniProt P13423 · UniProt P15917
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