Research workbench
Crystal structure of the protein-kinase a catalytic subunit from criteculus griseus in complex with compounds RKP032 and AMP
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
- 6EH2
- Type
- protein
- Length
- 363 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
- Ligands
- AMP
- Pockets
- 4 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Camp-dependent protein kinase catalytic subunit alpha (EC 2.7.11.11) | protein | 345 | 41% helix, 14% strand | P25321 |
| B | Camp-dependent protein kinase inhibitor | protein | 18 | 39% helix, 0% strand | — |
Ligands and binding sites
- AMP · Adenosine monophosphate · ligand · chains A
- 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
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 | 586 | 0.69 | 0.78 | 45 | AMP |
| 2 | 157 | 0.56 | 0.81 | 25 | MPD |
| 3 | 130 | 0.42 | 0.75 | 22 | empty |
| 4 | 50 | 0.30 | 0.76 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 728 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified (phosphorylation).
Compared structures
- 6EH2 · Crystal Structure of the Protein-Kinase A catalytic subunit from Criteculus Griseus in… · the same entry in another collection · chain B against B, 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 6EH2 · PDBe 6EH2 · UniProt P25321
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