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Crystal structure of casein kinase I delta (CK1D) with alphag-in conformation

Analyse Crystal structure of casein kinase I delta (CK1D) with alphag-in conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7P7H
Type
protein
Length
584 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Casein kinase I isoform delta
EC
2.7.11.1, 2.7.11.26
UniProt
P48730
Ligands
AMP
Pockets
6 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BCasein kinase I isoform delta (EC 2.7.11.1, 2.7.11.26)protein29239% helix, 18% strandP48730

Ligands and binding sites

  • AMP · Adenosine monophosphate · ligand · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15700.780.8466empty
22420.590.8034AMP
32190.580.7930AMP
42280.550.7840empty
5580.410.8111empty

Interfaces

1 interface between chains.

  • A–B · 663 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • 7P7H · Crystal structure of Casein Kinase I delta (CK1d) with alphaG-in conformation · the same entry in another collection · chain A against A, TM-score 1.00

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