Research workbench
Crystal structure of MOB1-LATS1 ntr domain complex
Analyse Crystal structure of MOB1-LATS1 ntr domain complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5B5W
- Type
- protein
- Length
- 236 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mob kinase activator 1B; SERINE/THREONINE-protein kinase LATS1
- EC
- 2.7.11.1
- UniProt
- Q8BPB0, O95835
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 66% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mob kinase activator 1B | protein | 172 | 58% helix, 2% strand | Q8BPB0 |
| U | SERINE/THREONINE-protein kinase LATS1 (EC 2.7.11.1) | protein | 64 | 88% helix, 0% strand | O95835 |
Ligands and binding sites
- ZN · Zinc ion · metal · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 302 | 0.68 | 0.83 | 32 | empty |
Interfaces
1 interface between chains.
- A–U · 1265 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 5B5W · Crystal structure of MOB1-LATS1 NTR domain complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q8BPB0 · AlphaFold monomer V2.0 prediction for mob kinase activator 1B (Q8BPB0) · a predicted model of the same protein · chain A against A, TM-score 0.95
- O95835 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase LATS1 (O95835) · a predicted model of the same protein · chain U against A, TM-score 0.85
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 Q8BPB0
- Every structure of UniProt O95835
- Elsewhere: RCSB PDB 5B5W · PDBe 5B5W · UniProt Q8BPB0 · UniProt O95835
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