MolNFT v1 · #170927 · protein
Crystal structure of camp-dependent protein kinase (PKA) in complex with the methylated fasudil-derived fragment N-methylisoquinoline-5- sulfonamide (soaked)
6YNC: “Crystal structure of camp-dependent protein kinase (PKA) in complex with the methylated fasudil-derived…”. X-ray diffraction, 1 ligand (7CT). MolNFT v1 #170927 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6YNC
- Type
- protein
- Length
- 364 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P25321, P63248
- Ligands
- 7CT
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 350 | — | P25321 |
| B | — | protein | 14 | — | P63248 |
Ligands and binding sites
- 7CT · ~{N}-methylisoquinoline-5-sulfonamide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6YNC · Crystal structure of cAMP-dependent Protein Kinase (PKA) in complex with the methylated… · the same entry in another collection · chain A against A, TM-score 1.00
- P63248 · AlphaFold monomer V2.0 prediction for camp-dependent protein kinase inhibitor alpha… · a predicted model of the same protein · chain B against A, TM-score 0.22
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 P25321
- Every structure of UniProt P63248
- Elsewhere: RCSB PDB 6YNC · PDBe 6YNC · UniProt P25321 · UniProt P63248
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