7P7G: Casein kinase I isoform delta

Crystal structure of phosphorylated pT220 Casein Kinase I delta (CK1d), conformation 2 and 3. Determined by X-ray diffraction at 1.7 Å resolution. Released 13 Apr 2022.

Method
X-ray diffraction
Resolution
1.7 Å
Organism
Homo sapiens
Chains
2
Atoms
5,215
Mol. weight
70.59 kDa
Ligands
CIT, AMP
Released
13 Apr 2022

Explore 7P7G in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7P7G contains 34 α-helices and 26 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 17 helices, 12 β-strands

ElementResiduesLengthSheet
β-strand9-18101
β-strand21-2881
β-strand33-4081
α-helix49-5810
β-strand68-7471
β-strand77-8261
β-strand8812
α-helix89-957
α-helix102-12120
β-strand124-12523
α-helix131-1333
β-strand134-13632
α-helix139-1413
β-strand145-14732
β-strand154-15523
β-strand15714
β-strand16414
α-helix165-1673
α-helix171-1733
α-helix182-1854
α-helix188-1903
α-helix192-20817
α-helix218-2192
α-helix226-2338
α-helix237-2404
α-helix247-25711
α-helix262-2643
α-helix266-27914
α-helix289-2924
Chain B: 17 helices, 14 β-strands
ElementResiduesLengthSheet
β-strand9-1795
β-strand22-2875
β-strand33-4195
α-helix49-5911
β-strand68-7475
β-strand77-8375
β-strand8816
α-helix89-957
α-helix102-12120
β-strand124-12527
α-helix131-1333
β-strand134-13636
α-helix139-1413
α-helix1441
β-strand145-14736
β-strand154-15527
β-strand15718
α-helix1631
β-strand16418
α-helix165-1662
β-strand16919
α-helix182-1854
β-strand18819
α-helix189-1902
α-helix192-20817
α-helix221-23313
α-helix237-2404
α-helix247-25711
α-helix262-2643
α-helix266-28015
α-helix289-2913

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Casein kinase I isoform deltaA, Bprotein296Homo sapiensP48730 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>7P7G_1 Casein kinase I isoform delta (chains A, B)
SMMELRVGNRYRLGRKIGSGSFGDIYLGTDIAAGEEVAIKLECVKTKHPQLHIESKIYKM
MQGGVGIPTIRWCGAEGDYNVMVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEY
IHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDARTHQHIPYRENKNLTGTAR
YASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIE
VLCKGYPSEFATYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGFSYDYVFDWNMLK

Ligands and cofactors

IDNameFormulaCopies
CITCitric acidC6 H8 O73
AMPAdenosine monophosphateC10 H14 N5 O7 P2

Water and common crystallization additives (EDO) are not listed.

Primary citation

Kinase domain autophosphorylation rewires the activity and substrate specificity of CK1 enzymes. Cullati, S.N., Chaikuad, A., Chen, J.S. et al. Mol Cell (2022) 82:2006. DOI 10.1016/j.molcel.2022.03.005 · PubMed

Other PDB entries of the same protein (UniProt P48730 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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