MolNFT v1 · #17723 · protein
Crystal structure of the human Y14/MAGOH complex
1P27 · Mago nashi protein homolog: “Crystal structure of the human Y14/MAGOH complex”. X-ray diffraction, 9 pockets (best druggability 0.70). MolNFT v1 #17723 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1P27
- Type
- protein
- Length
- 472 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mago nashi protein homolog; RNA-binding protein 8A
- UniProt
- P61326, Q9Y5S9
- Pockets
- 9 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 29% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Mago nashi protein homolog | protein | 144 | 33% helix, 36% strand | P61326 |
| B, D | RNA-binding protein 8A | protein | 92 | 24% helix, 37% strand | Q9Y5S9 |
Pockets
9 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 143 | 0.70 | 0.90 | 36 | empty |
| 2 | 296 | 0.57 | 0.77 | 24 | empty |
| 3 | 167 | 0.46 | 0.76 | 27 | empty |
| 4 | 131 | 0.41 | 0.75 | 22 | empty |
| 5 | 98 | 0.37 | 0.75 | 25 | empty |
Interfaces
3 interfaces between chains.
- C–D · 1214 Ų buried · 18 hydrogen bonds · protein-protein
- A–B · 1195 Ų buried · 14 hydrogen bonds · protein-protein
- A–C · 821 Ų buried · 20 hydrogen bonds · protein-protein
Compared structures
- 1P27 · Crystal Structure of the Human Y14/Magoh complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q9Y5S9 · AlphaFold monomer V2.0 prediction for RNA-binding protein 8A (Q9Y5S9) · a predicted model of the same protein · chain B against A, TM-score 0.99
- P61326 · AlphaFold monomer V2.0 prediction for protein mago nashi homolog (P61326) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P61326
- Every structure of UniProt Q9Y5S9
- Elsewhere: RCSB PDB 1P27 · PDBe 1P27 · UniProt P61326 · UniProt Q9Y5S9
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