MolNFT v1 · #115224 · protein
Crystal structure of the ntd of drosophila oskar protein
5CD8 · Maternal effect protein oskar: “Crystal structure of the ntd of drosophila oskar protein”. X-ray diffraction, 4 pockets (best druggability 0.79). MolNFT v1 #115224 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5CD8
- Type
- protein
- Length
- 440 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Maternal effect protein oskar
- UniProt
- P25158
- Pockets
- 4 · best druggability 0.79
Structure
x-ray diffraction · 4 distinct chains · 42% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Maternal effect protein oskar | protein | 76 | 41% helix, 14% strand | P25158 |
| B, C | Maternal effect protein oskar | protein | 74 | 43% helix, 12% strand | P25158 |
| D, F | Maternal effect protein oskar | protein | 73 | 42% helix, 12% strand | P25158 |
| E | Maternal effect protein oskar | protein | 70 | 43% helix, 16% strand | P25158 |
Ligands and binding sites
- GOL · Glycerol · additive · 2 copies · chains A, E, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 962 | 0.79 | 0.81 | 86 | GOL |
| 2 | 210 | 0.54 | 0.78 | 22 | empty |
| 3 | 103 | 0.38 | 0.76 | 16 | empty |
| 4 | 71 | 0.30 | 0.74 | 20 | empty |
Interfaces
10 interfaces between chains.
- E–F · 691 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 627 Ų buried · 11 hydrogen bonds · protein-protein
- C–D · 592 Ų buried · 12 hydrogen bonds · protein-protein
- A–E · 355 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 230 Ų buried · 5 hydrogen bonds · protein-protein
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 P25158
- Elsewhere: RCSB PDB 5CD8 · PDBe 5CD8 · UniProt P25158
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