Research workbench
Apo crystal structure of the protein-kinase a catalytic subunit from criteculus
Analyse Apo crystal structure of the protein-kinase a catalytic subunit from criteculus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6EH0
- Type
- protein
- Length
- 339 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Camp-dependent protein kinase catalytic subunit alpha
- EC
- 2.7.11.11
- UniProt
- P25321
- Pockets
- 3 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Camp-dependent protein kinase catalytic subunit alpha (EC 2.7.11.11) | protein | 339 | 38% helix, 15% strand | P25321 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 299 | 0.67 | 0.82 | 36 | empty |
| 2 | 85 | 0.46 | 0.80 | 12 | empty |
| 3 | 58 | 0.31 | 0.76 | 17 | empty |
Modifications
Observed in the structure: 3 modified (phosphorylation).
Compared structures
- 6EH0 · Apo crystal structure of the Protein-Kinase A catalytic subunit from Criteculus · 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 P25321
- Elsewhere: RCSB PDB 6EH0 · PDBe 6EH0 · UniProt P25321
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