Research workbench
Human MOB1-phosphopeptide complex
Analyse Human MOB1-phosphopeptide complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4JIZ
- Type
- protein
- Length
- 180 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mob kinase activator 1A; Phosphopeptide
- UniProt
- Q9H8S9
- Ligands
- ZN
Structure
x-ray diffraction · 2 distinct chains · 59% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mob kinase activator 1A | protein | 172 | 62% helix, 3% strand | Q9H8S9 |
| B | Phosphopeptide | protein | 8 | 0% helix, 38% strand | — |
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.
Interfaces
1 interface between chains.
- A–B · 522 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
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
- Elsewhere: RCSB PDB 4JIZ · PDBe 4JIZ · UniProt Q9H8S9
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