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Y41 and T47 phosphorylation of the mengovirus leader protein: NMR studies of the phosphorylation of the mengovirus leader protein reveal stabilization of intermolecular domain interactions
Analyse Y41 and T47 phosphorylation of the mengovirus leader protein: NMR studies of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2MMK
- Type
- protein
- Length
- 71 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Leader protein
- UniProt
- P12296
- Ligands
- ZN
Structure
solution nmr · 1 distinct chain · 6% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Leader protein | protein | 71 | 6% helix, 3% strand | P12296 |
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.
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 2MMK · Y41 and T47 phosphorylation of the Mengovirus Leader Protein: NMR Studies of the… · the same entry in another collection · chain A against A, 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 P12296
- Elsewhere: RCSB PDB 2MMK · PDBe 2MMK · UniProt P12296
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