Research workbench
Crystal structure of the drosophila mago nashi-Y14 complex
Analyse Crystal structure of the drosophila mago nashi-Y14 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1OO0
- Type
- protein
- Length
- 236 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mago nashi protein; CG8781-pa
- UniProt
- P49028, Q9V535
- Ligands
- SR
- Pockets
- 2 · best druggability 0.37
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mago nashi protein | protein | 144 | 34% helix, 35% strand | P49028 |
| B | CG8781-pa | protein | 92 | 24% helix, 35% strand | Q9V535 |
Ligands and binding sites
- SR · Strontium ion · metal · chains A
- BME · Beta-mercaptoethanol · additive · 2 copies · chains A, B
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 2 copies · chains A
- GOL · Glycerol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 86 | 0.37 | 0.77 | 19 | empty |
| 2 | 73 | 0.36 | 0.77 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1209 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (additive adduct).
Compared structures
- 1OO0 · Crystal structure of the Drosophila Mago nashi-Y14 complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q9V535 · AlphaFold monomer V2.0 prediction for RNA-binding protein 8A (Q9V535) · a predicted model of the same protein · chain B against A, TM-score 0.97
- P49028 · AlphaFold monomer V2.0 prediction for protein mago nashi (P49028) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 P49028
- Every structure of UniProt Q9V535
- Elsewhere: RCSB PDB 1OO0 · PDBe 1OO0 · UniProt P49028 · UniProt Q9V535
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