Research workbench
Crystal structure of the protein-kinase a catalytic subunit from criteculus griseus in complex with compounds RKP241 and fasudil
Analyse 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
- 5OK3
- Type
- protein
- Length
- 371 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Camp-dependent protein kinase catalytic subunit alpha; UPF0418 protein FAM164A
- EC
- 2.7.11.11
- UniProt
- P25321, G3HK48
- Ligands
- M77
- Pockets
- 4 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Camp-dependent protein kinase catalytic subunit alpha (EC 2.7.11.11) | protein | 353 | 41% helix, 15% strand | P25321 |
| D | UPF0418 protein FAM164A | protein | 18 | 39% helix, 0% strand | G3HK48 |
Ligands and binding sites
- M77 · 5-(1,4-diazepan-1-sulfonyl)isoquinoline · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 514 | 0.75 | 0.83 | 53 | M77 |
| 2 | 151 | 0.58 | 0.82 | 20 | empty |
| 3 | 112 | 0.38 | 0.75 | 24 | empty |
| 4 | 77 | 0.32 | 0.74 | 16 | empty |
Interfaces
1 interface between chains.
- A–D · 880 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 modified (phosphorylation, nonstandard).
Compared structures
- 5OK3 · Crystal Structure of the Protein-Kinase A catalytic subunit from Criteculus Griseus in… · 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
- Every structure of UniProt G3HK48
- Elsewhere: RCSB PDB 5OK3 · PDBe 5OK3 · UniProt P25321 · UniProt G3HK48
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