Research workbench
The S31N mutant of the influenza a M2 proton channel in two distinct conformational states
Analyse The S31N mutant of the influenza a M2 proton channel in two distinct… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6MJH
- Type
- protein
- Length
- 200 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Matrix protein 2
- UniProt
- A0A0R5TVW3
- Ligands
- ACE, CA, NH2, CL
- Pockets
- 4 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 84% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | Matrix protein 2 | protein | 25 | 84% helix, 0% strand | A0A0R5TVW3 |
Ligands and binding sites
- ACE · Acetyl group · ligand · 8 copies · chains A, B, C, D, E, H, F, G
- CA · Calcium ion · metal · 4 copies · chains A, B, C, D, H, E, F, G
- NH2 · Amino group · ion · 8 copies · chains A, H, B, C, D, E, F, G
- CL · Chloride ion · ion · chains E, F, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 158 | 0.80 | 0.96 | 35 | empty |
| 2 | 647 | 0.79 | 0.84 | 32 | empty |
| 3 | 363 | 0.68 | 0.80 | 33 | empty |
| 4 | 60 | 0.35 | 0.77 | 16 | empty |
Interfaces
16 interfaces between chains.
- A–B · 502 Ų buried · 5 hydrogen bonds · protein-protein
- C–D · 492 Ų buried · 6 hydrogen bonds · protein-protein
- A–D · 491 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 486 Ų buried · 6 hydrogen bonds · protein-protein
- E–F · 375 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 covalent (covalent ligand).
Compared structures
- 6MJH · The S31N mutant of the influenza A M2 proton channel in two distinct conformational states · the same entry in another collection · chain A against A, 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 A0A0R5TVW3
- Elsewhere: RCSB PDB 6MJH · PDBe 6MJH · UniProt A0A0R5TVW3
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