Research workbench
Structure of strad and MO25
Analyse Structure of strad and MO25 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3GNI
- Type
- protein
- Length
- 639 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein MO25; Strad alpha
- UniProt
- Q9Y376, Q7RTN6
- Ligands
- ATP
- Pockets
- 8 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 55% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein MO25 | protein | 335 | 73% helix, 1% strand | Q9Y376 |
| B | Strad alpha | protein | 304 | 36% helix, 19% strand | Q7RTN6 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1141 | 0.75 | 0.77 | 94 | empty |
| 2 | 453 | 0.71 | 0.81 | 60 | ATP |
| 3 | 339 | 0.58 | 0.76 | 34 | empty |
| 4 | 148 | 0.43 | 0.75 | 23 | empty |
| 5 | 88 | 0.36 | 0.76 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 2085 Ų buried · 35 hydrogen bonds · protein-protein
Compared structures
- 3GNI · Structure of STRAD and MO25 · the same entry in another collection · chain A against A, TM-score 1.00
- Q9Y376 · AlphaFold monomer V2.0 prediction for calcium-binding protein 39 (Q9Y376) · a predicted model of the same protein · chain A against A, TM-score 0.96
- Q7RTN6 · AlphaFold monomer V2.0 prediction for STE20-related kinase adapter protein alpha (Q7RTN6) · a predicted model of the same protein · chain B against A, TM-score 0.93
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 Q9Y376
- Every structure of UniProt Q7RTN6
- Elsewhere: RCSB PDB 3GNI · PDBe 3GNI · UniProt Q9Y376 · UniProt Q7RTN6
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