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The molecular basis for protein kinase a anchoring revealed by solution NMR
Analyse The molecular basis for protein kinase a anchoring revealed by solution NMR in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1R2A
- Type
- protein
- Length
- 92 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (camp-dependent protein kinase type II regulatory subunit)
- EC
- 2.7.1.37
- UniProt
- P12367
Structure
solution nmr · 1 distinct chain · 63% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protein (camp-dependent protein kinase type II regulatory subunit) (EC 2.7.1.37) | protein | 46 | 63% helix, 0% strand | P12367 |
Interfaces
1 interface between chains.
- A–B · 827 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 1R2A · The molecular basis for protein kinase a anchoring revealed by solution NMR · the same entry in another collection · chain B against B, TM-score 1.00
- P12367 · AlphaFold monomer V2.0 prediction for camp-dependent protein kinase type II-alpha… · a predicted model of the same protein · chain A against A, TM-score 0.73
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 P12367
- Elsewhere: RCSB PDB 1R2A · PDBe 1R2A · UniProt P12367
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