MolNFT v1 · #172898 · protein
Alpha-hemolysin from staphylococcus aureus
7AHL: “Alpha-hemolysin from staphylococcus aureus”. X-ray diffraction, 20 pockets (best druggability 0.75). MolNFT v1 #172898 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7AHL
- Type
- protein
- Length
- 2,051 residues
- Chains
- 7
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-hemolysin
- UniProt
- P09616
- Pockets
- 20 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 5% helix, 58% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G | Alpha-hemolysin | protein | 293 | 5% helix, 58% strand | P09616 |
Pockets
20 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 654 | 0.75 | 0.81 | 68 | empty |
| 2 | 853 | 0.75 | 0.79 | 102 | empty |
| 3 | 665 | 0.74 | 0.80 | 70 | empty |
| 4 | 777 | 0.73 | 0.79 | 87 | empty |
| 5 | 553 | 0.72 | 0.80 | 69 | empty |
Interfaces
15 interfaces between chains.
- B–C · 2997 Ų buried · 57 hydrogen bonds · protein-protein
- F–G · 2965 Ų buried · 59 hydrogen bonds · protein-protein
- D–E · 2945 Ų buried · 58 hydrogen bonds · protein-protein
- A–B · 2945 Ų buried · 54 hydrogen bonds · protein-protein
- C–D · 2939 Ų buried · 56 hydrogen bonds · protein-protein
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 P09616
- Elsewhere: RCSB PDB 7AHL · PDBe 7AHL · UniProt P09616
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