Research workbench
Crystal structure of protein kinase a in complex with pyridine-pyrazolopyridine based inhibitors
Analyse Crystal structure of protein kinase a in complex with pyridine-pyrazolopyridine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2OH0
- Type
- protein
- Length
- 356 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Camp-dependent protein kinase, alpha-catalytic subunit; Inhibitory peptide
- EC
- 2.7.11.11
- UniProt
- P00517
- Ligands
- 2PY
- Pockets
- 6 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | Camp-dependent protein kinase, alpha-catalytic subunit (EC 2.7.11.11) | protein | 336 | 38% helix, 16% strand | P00517 |
| I | Inhibitory peptide | protein | 20 | 35% helix, 5% strand | — |
Ligands and binding sites
- 2PY · (2S)-1-{[5-(1H-indazol-5-yl)pyridin-3-yl]oxy}-3-[(7AS)-7AH-indol-3-yl]propan-2-amine · ligand · chains E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 458 | 0.81 | 0.88 | 41 | 2PY |
| 2 | 119 | 0.50 | 0.81 | 19 | empty |
| 3 | 67 | 0.42 | 0.80 | 11 | empty |
| 4 | 88 | 0.36 | 0.75 | 19 | empty |
| 5 | 71 | 0.29 | 0.73 | 17 | empty |
Interfaces
1 interface between chains.
- E–I · 1011 Ų buried · 21 hydrogen bonds · protein-protein
Compared structures
- 2OH0 · Crystal structure of Protein Kinase A in complex with Pyridine-Pyrazolopyridine Based… · the same entry in another collection · chain E against E, 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 P00517
- Elsewhere: RCSB PDB 2OH0 · PDBe 2OH0 · UniProt P00517
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