MolNFT v1 · #147927 · protein
Crystal structure of the protein-kinase a catalytic subunit from criteculus griseus in complex with compounds RKP013
6ERV · Camp-dependent protein kinase catalytic subunit alpha: “Crystal structure of the protein-kinase a catalytic subunit from criteculus griseus in complex with compounds…”. X-ray diffraction, 2 pockets (best druggability 0.70). MolNFT…
- PDB
- 6ERV
- Type
- protein
- Length
- 361 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Camp-dependent protein kinase catalytic subunit alpha; Camp-dependent protein kinase…
- EC
- 2.7.11.11
- UniProt
- P25321, A0A061IH64
- Pockets
- 2 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 41% 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 | 343 | 41% helix, 15% strand | P25321 |
| B | Camp-dependent protein kinase inhibitor | protein | 18 | 39% helix, 0% strand | A0A061IH64 |
Ligands and binding sites
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 625 | 0.70 | 0.78 | 53 | empty |
| 2 | 166 | 0.57 | 0.81 | 23 | MPD |
Interfaces
1 interface between chains.
- A–B · 792 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (phosphorylation).
Compared structures
- 6ERV · 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 A0A061IH64
- Elsewhere: RCSB PDB 6ERV · PDBe 6ERV · UniProt P25321 · UniProt A0A061IH64
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