Research workbench
Structural basis for MOB1-dependent activation of the core mst-lats kinase cascade in hippo signaling
Analyse Structural basis for MOB1-dependent activation of the core mst-lats kinase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5BRM
- Type
- protein
- Length
- 1,060 residues
- Chains
- 15
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mob kinase activator 1A; SERINE/THREONINE-protein kinase 3
- EC
- 2.7.11.1
- UniProt
- Q9H8S9, Q13188
- Ligands
- ZN
- Pockets
- 18 · best druggability 0.72
Structure
x-ray diffraction · 13 distinct chains · 54% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mob kinase activator 1A | protein | 154 | 62% helix, 5% strand | Q9H8S9 |
| B | Mob kinase activator 1A | protein | 158 | 60% helix, 4% strand | Q9H8S9 |
| C, E, F | Mob kinase activator 1A | protein | 160 | 59% helix, 3% strand | Q9H8S9 |
| D | Mob kinase activator 1A | protein | 144 | 65% helix, 2% strand | Q9H8S9 |
| G | SERINE/THREONINE-protein kinase 3 (EC 2.7.11.1) | protein | 22 | 14% helix, 14% strand | Q13188 |
| H | SERINE/THREONINE-protein kinase 3 (EC 2.7.11.1) | protein | 17 | 24% helix, 18% strand | Q13188 |
| I | SERINE/THREONINE-protein kinase 3 (EC 2.7.11.1) | protein | 12 | 42% helix, 17% strand | Q13188 |
| J | SERINE/THREONINE-protein kinase 3 (EC 2.7.11.1) | protein | 13 | 31% helix, 15% strand | Q13188 |
| K | SERINE/THREONINE-protein kinase 3 (EC 2.7.11.1) | protein | 11 | 36% helix, 9% strand | Q13188 |
| L | SERINE/THREONINE-protein kinase 3 (EC 2.7.11.1) | protein | 12 | 25% helix, 17% strand | Q13188 |
| M | SERINE/THREONINE-protein kinase 3 (EC 2.7.11.1) | protein | 17 | 0% helix, 0% strand | Q13188 |
| N | SERINE/THREONINE-protein kinase 3 (EC 2.7.11.1) | protein | 12 | 0% helix, 0% strand | Q13188 |
| O | SERINE/THREONINE-protein kinase 3 (EC 2.7.11.1) | protein | 8 | 0% helix, 0% strand | Q13188 |
Ligands and binding sites
- ZN · Zinc ion · metal · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 612 | 0.72 | 0.79 | 61 | empty |
| 2 | 415 | 0.68 | 0.80 | 46 | empty |
| 3 | 53 | 0.67 | 0.96 | 16 | empty |
| 4 | 109 | 0.62 | 0.87 | 29 | empty |
| 5 | 447 | 0.61 | 0.75 | 45 | empty |
Interfaces
23 interfaces between chains.
- A–G · 999 Ų buried · 18 hydrogen bonds · protein-protein
- B–H · 972 Ų buried · 17 hydrogen bonds · protein-protein
- B–C · 876 Ų buried · 8 hydrogen bonds · protein-protein
- F–L · 869 Ų buried · 10 hydrogen bonds · protein-protein
- D–J · 855 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (phosphorylation).
Compared structures
- 5BRM · Structural basis for Mob1-dependent activation of the core Mst-Lats kinase cascade in… · the same entry in another collection · chain K against K, TM-score 1.00
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 Q9H8S9
- Every structure of UniProt Q13188
- Elsewhere: RCSB PDB 5BRM · PDBe 5BRM · UniProt Q9H8S9 · UniProt Q13188
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