Research workbench
Crystal structure of the M113N mutant of alpha-hemolysin
Analyse Crystal structure of the M113N mutant of alpha-hemolysin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3M4D
- 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 0.80
Structure
x-ray diffraction · 1 distinct chain · 5% helix, 59% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G | Alpha-hemolysin | protein | 293 | 5% helix, 59% strand | P09616 |
Pockets
20 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1029 | 0.80 | 0.81 | 113 | empty |
| 2 | 864 | 0.78 | 0.81 | 97 | empty |
| 3 | 910 | 0.75 | 0.78 | 89 | empty |
| 4 | 621 | 0.72 | 0.80 | 61 | empty |
| 5 | 761 | 0.72 | 0.78 | 79 | empty |
Interfaces
14 interfaces between chains.
- C–D · 2980 Ų buried · 67 hydrogen bonds · protein-protein
- A–G · 2933 Ų buried · 63 hydrogen bonds · protein-protein
- D–E · 2918 Ų buried · 65 hydrogen bonds · protein-protein
- A–B · 2899 Ų buried · 64 hydrogen bonds · protein-protein
- F–G · 2896 Ų buried · 63 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 3M4D · PDBe 3M4D · UniProt P09616
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