Research workbench
A kinase complex MST4-MOB4
Analyse A kinase complex MST4-MOB4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5YF4
- Type
- protein
- Length
- 140 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mob-like protein phocein; Peptide from SERINE/THREONINE-protein kinase 26
- EC
- 2.7.11.1
- UniProt
- Q9Y3A3, Q9P289
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.42
Structure
x-ray diffraction · 2 distinct chains · 59% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mob-like protein phocein | protein | 129 | 64% helix, 5% strand | Q9Y3A3 |
| B | Peptide from SERINE/THREONINE-protein kinase 26 (EC 2.7.11.1) | protein | 11 | 0% helix, 27% strand | Q9P289 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 82 | 0.42 | 0.79 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 570 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 5YF4 · A kinase complex MST4-MOB4 · the same entry in another collection · chain A against A, TM-score 1.00
- Q9Y3A3 · AlphaFold monomer V2.0 prediction for mob-like protein phocein (Q9Y3A3) · a predicted model of the same protein · chain A against A, TM-score 0.97
- Q9P289 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase 26 (Q9P289) · a predicted model of the same protein · chain B against A, TM-score 0.25
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 Q9Y3A3
- Every structure of UniProt Q9P289
- Elsewhere: RCSB PDB 5YF4 · PDBe 5YF4 · UniProt Q9Y3A3 · UniProt Q9P289
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