MolNFT v1 · #36510 · protein
Protein kinase a bound to (S)-2-(1H-indol-3-yl)-1-[5-((E)-2- pyridin-4-yl-vinyl)-pyridin-3-yloxymethyl]-ethylamine
2F7X · Camp-dependent protein kinase, alpha-catalytic subunit: “Protein kinase a bound to (S)-2-(1H-indol-3-yl)-1-[5-((E)-2…”. X-ray diffraction, 1 ligand (4EA), 6 pockets (best druggability 0.79). MolNFT v1 #36510 on GenesisL1: 3D…
- PDB
- 2F7X
- 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; Pki, inhibitory peptide
- EC
- 2.7.1.37
- UniProt
- P00517
- Ligands
- 4EA
- Pockets
- 6 · best druggability 0.79
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 2.7.1.37) | protein | 336 | 38% helix, 16% strand | P00517 |
| I | Pki, inhibitory peptide | protein | 20 | 35% helix, 5% strand | — |
Ligands and binding sites
- 4EA · (1S)-2-(1H-indol-3-yl)-1-[({5-[(E)-2-pyridin-4-ylvinyl]pyridin-3-yl}oxy)methyl]ethylamine · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 458 | 0.79 | 0.86 | 44 | 4EA |
| 2 | 101 | 0.46 | 0.80 | 16 | empty |
| 3 | 72 | 0.45 | 0.81 | 11 | empty |
| 4 | 93 | 0.41 | 0.78 | 20 | empty |
| 5 | 60 | 0.30 | 0.74 | 12 | empty |
Interfaces
1 interface between chains.
- E–I · 988 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 2F7X · Protein Kinase A bound to (S)-2-(1H-Indol-3-yl)-1-[5-((E)-2-pyridin-4-yl-vinyl)-pyridin-3… · 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 2F7X · PDBe 2F7X · UniProt P00517
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