Research workbench
M3-MT4L receptor bound to nms
Analyse M3-MT4L receptor bound to nms in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4U16
- Type
- protein
- Length
- 773 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Muscarinic acetylcholine receptor M3,LYSOZYME,MUSCARINIC acetylcholine receptor M3
- EC
- 3.2.1.17
- UniProt
- P08483, D9IEF7
- Ligands
- 3C0
- Pockets
- 10 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 75% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Muscarinic acetylcholine receptor M3,LYSOZYME,MUSCARINIC acetylcholine receptor M3 (EC 3.2.1.17) | protein | 381 | 75% helix, 0% strand | P08483, D9IEF7 |
| B | Muscarinic acetylcholine receptor M3,LYSOZYME,MUSCARINIC acetylcholine receptor M3 (EC 3.2.1.17) | protein | 392 | 75% helix, 0% strand | P08483, D9IEF7 |
Ligands and binding sites
- 3C0 · N-methyl scopolamine · ligand · 2 copies · chains A, B
- TAR · D(-)-tartaric acid · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1200 | 0.84 | 0.84 | 80 | empty |
| 2 | 591 | 0.81 | 0.86 | 55 | 3C0 |
| 3 | 517 | 0.79 | 0.86 | 43 | 3C0 |
| 4 | 447 | 0.67 | 0.79 | 61 | empty |
| 5 | 147 | 0.59 | 0.83 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 913 Ų buried · 1 hydrogen bond · 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 P08483
- Every structure of UniProt D9IEF7
- Elsewhere: RCSB PDB 4U16 · PDBe 4U16 · UniProt P08483 · UniProt D9IEF7
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