MolNFT v1 · #107201 · protein
Ebola virus VP24 in complex with karyopherin alpha 5 C-terminus
4U2X · Membrane-associated protein VP24: “Ebola virus VP24 in complex with karyopherin alpha 5 C-terminus”. X-ray diffraction, 1 ligand (CL), 13 pockets (best druggability 0.60). MolNFT v1 #107201 on GenesisL1: 3D structure, binding sites…
- PDB
- 4U2X
- Type
- protein
- Length
- 1,162 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Membrane-associated protein VP24; Importin subunit alpha-6
- UniProt
- Q05322, O15131
- Ligands
- CL
- Pockets
- 13 · best druggability 0.60
Structure
x-ray diffraction · 6 distinct chains · 58% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Membrane-associated protein VP24 | protein | 216 | 43% helix, 20% strand | Q05322 |
| B | Membrane-associated protein VP24 | protein | 215 | 43% helix, 20% strand | Q05322 |
| C | Membrane-associated protein VP24 | protein | 213 | 44% helix, 21% strand | Q05322 |
| D | Importin subunit alpha-6 | protein | 170 | 76% helix, 0% strand | O15131 |
| E | Importin subunit alpha-6 | protein | 173 | 76% helix, 0% strand | O15131 |
| F | Importin subunit alpha-6 | protein | 175 | 75% helix, 0% strand | O15131 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 417 | 0.60 | 0.76 | 42 | empty |
| 2 | 197 | 0.59 | 0.81 | 33 | empty |
| 3 | 387 | 0.57 | 0.74 | 40 | empty |
| 4 | 178 | 0.55 | 0.80 | 20 | empty |
| 5 | 220 | 0.55 | 0.78 | 34 | empty |
Interfaces
6 interfaces between chains.
- B–E · 1162 Ų buried · 15 hydrogen bonds · protein-protein
- A–D · 1159 Ų buried · 19 hydrogen bonds · protein-protein
- C–F · 1114 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 813 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 310 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 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 Q05322
- Every structure of UniProt O15131
- Elsewhere: RCSB PDB 4U2X · PDBe 4U2X · UniProt Q05322 · UniProt O15131
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