Research workbench
Proaerolysin mutant W373L
Analyse Proaerolysin mutant W373L in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Z52
- Type
- protein
- Length
- 901 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aerolysin
- UniProt
- P09167
- Pockets
- 9 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 18% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aerolysin | protein | 451 | 17% helix, 39% strand | P09167 |
| B | Aerolysin | protein | 450 | 18% helix, 40% strand | P09167 |
Pockets
9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 842 | 0.80 | 0.83 | 110 | empty |
| 2 | 755 | 0.79 | 0.83 | 83 | empty |
| 3 | 392 | 0.65 | 0.79 | 46 | empty |
| 4 | 237 | 0.60 | 0.80 | 35 | empty |
| 5 | 268 | 0.59 | 0.79 | 37 | empty |
Interfaces
1 interface between chains.
- A–B · 2658 Ų buried · 29 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
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 P09167
- Elsewhere: RCSB PDB 1Z52 · PDBe 1Z52 · UniProt P09167
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