Research workbench
Crystal structure of ARG280ALA mutant of catalytic subunit of camp- dependent protein kinase
Analyse Crystal structure of ARG280ALA mutant of catalytic subunit of camp- dependent… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QAL
- Type
- protein
- Length
- 359 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Camp-dependent protein kinase catalytic subunit alpha; Protein kinase inhibitor
- EC
- 2.7.11.11
- UniProt
- P05132, Q3UTL0
- Ligands
- ATP, MG
- Pockets
- 6 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | Camp-dependent protein kinase catalytic subunit alpha (EC 2.7.11.11) | protein | 341 | 36% helix, 15% strand | P05132 |
| I | Protein kinase inhibitor | protein | 18 | 33% helix, 0% strand | Q3UTL0 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · chains E, I
- MG · Magnesium ion · metal · 2 copies · 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 | 160 | 0.82 | 0.97 | 31 | ATP, MG |
| 2 | 84 | 0.45 | 0.80 | 13 | empty |
| 3 | 51 | 0.39 | 0.81 | 18 | empty |
| 4 | 86 | 0.36 | 0.76 | 19 | empty |
| 5 | 88 | 0.33 | 0.74 | 20 | empty |
Interfaces
1 interface between chains.
- E–I · 946 Ų buried · 25 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 3QAL · Crystal Structure of Arg280Ala mutant of Catalytic subunit of cAMP-dependent Protein… · 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 P05132
- Every structure of UniProt Q3UTL0
- Elsewhere: RCSB PDB 3QAL · PDBe 3QAL · UniProt P05132 · UniProt Q3UTL0
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