Research workbench
Cryo-EM structure of murine dispatched nnn mutant
Analyse Cryo-EM structure of murine dispatched nnn mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7RPJ
- Type
- protein
- Length
- 926 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein dispatched homolog 1
- UniProt
- Q3TDN0
- Ligands
- Y01, NAG
- Pockets
- 13 · best druggability 0.65
Structure
electron microscopy · 1 distinct chain · 60% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein dispatched homolog 1 | protein | 926 | 60% helix, 7% strand | Q3TDN0 |
Ligands and binding sites
- Y01 · Cholesterol hemisuccinate · ligand · 14 copies · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 236 | 0.65 | 0.83 | 35 | empty |
| 2 | 134 | 0.63 | 0.86 | 23 | empty |
| 3 | 170 | 0.61 | 0.83 | 26 | empty |
| 4 | 363 | 0.59 | 0.76 | 35 | Y01 |
| 5 | 321 | 0.57 | 0.76 | 41 | empty |
Modifications
Observed in the structure: 9 disulfide, 5 glycan (disulfide, N-glycosylation).
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 Q3TDN0
- Elsewhere: RCSB PDB 7RPJ · PDBe 7RPJ · UniProt Q3TDN0
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