Research workbench
Cryo-EM structure of HDISP1NNN-3C
Analyse Cryo-EM structure of HDISP1NNN-3C in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7E2G
- Type
- protein
- Length
- 901 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein dispatched homolog 1,PROTEIN dispatched homolog 1
- UniProt
- Q96F81
- Ligands
- Y01, NAG
- Pockets
- 14 · best druggability 0.72
Structure
electron microscopy · 1 distinct chain · 52% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D | Protein dispatched homolog 1,PROTEIN dispatched homolog 1 | protein | 901 | 52% helix, 4% strand | Q96F81 |
Ligands and binding sites
- Y01 · Cholesterol hemisuccinate · ligand · 11 copies · chains D
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 277 | 0.72 | 0.86 | 32 | empty |
| 2 | 195 | 0.60 | 0.82 | 29 | empty |
| 3 | 104 | 0.58 | 0.85 | 25 | empty |
| 4 | 169 | 0.57 | 0.81 | 27 | empty |
| 5 | 286 | 0.55 | 0.76 | 25 | empty |
Modifications
Observed in the structure: 4 glycan (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 Q96F81
- Elsewhere: RCSB PDB 7E2G · PDBe 7E2G · UniProt Q96F81
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