Research workbench
Ligand-receptor complex.
Analyse Ligand-receptor complex. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5MR9
- Type
- protein
- Length
- 200 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Neurturin
- UniProt
- Q99748
- Pockets
- 2 · best druggability 0.38
Structure
x-ray diffraction · 2 distinct chains · 15% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Neurturin | protein | 99 | 15% helix, 39% strand | Q99748 |
| B | Neurturin | protein | 101 | 15% helix, 40% strand | Q99748 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 84 | 0.38 | 0.77 | 19 | empty |
| 2 | 51 | 0.35 | 0.80 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 2141 Ų buried · 35 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 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 Q99748
- Elsewhere: RCSB PDB 5MR9 · PDBe 5MR9 · UniProt Q99748
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