3C0I: Peripheral plasma membrane protein CASK

CASK CaM-Kinase Domain- 3'-AMP complex, P212121 form. Determined by X-ray diffraction at 1.85 Å resolution. Released 29 Apr 2008.

Method: X-ray diffraction
Resolution: 1.85 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,737
Mol. weight: 39.6 kDa
Ligands: 3AM
Released: 29 Apr 2008

Explore 3C0I in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3C0I contains 20 α-helices and 13 β-strands across 1 chain. 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: 20 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	8-11	4
β-strand	12-20	9	1
β-strand	24-31	8	1
β-strand	37-44	8	1
α-helix	45-49	5
α-helix	56-68	13
β-strand	74	1	2
α-helix	75-76	2
β-strand	77-83	7	1
β-strand	86-92	7	1
α-helix	93-94	2
β-strand	98	1	2
α-helix	99-108	10
α-helix	115-134	20
β-strand	137-138	2	3
α-helix	144-146	3
β-strand	147-149	3	2
α-helix	156-157	2
β-strand	158-160	3	2
β-strand	167-168	2	3
β-strand	175	1	4
α-helix	183-185	3
α-helix	188-191	4
β-strand	196	1	4
α-helix	199-214	16
α-helix	223-232	10
α-helix	239-242	4
α-helix	247-256	10
α-helix	265-266	2
α-helix	267-271	5
α-helix	274-277	4
α-helix	279-282	4
α-helix	289-302	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Peripheral plasma membrane protein CASK	A	protein	351	Homo sapiens	O14936 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3C0I_1 Peripheral plasma membrane protein CASK (chains A)
GSPGISGGGGGILDMADDDVLFEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVA
KFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLCFEIVKR
ADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVA
IQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERL
FEGIIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERDRYAYKI
HLPETVEQLRKFNARRKLKGAVLAAVSSHKFNSFYGDPPEELPDFSEDPTS

Ligands and cofactors

ID	Name	Formula	Copies
3AM	[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-4-hydroxy-2-(hydroxymethyl)oxolan-3-yl]…	C10 H14 N5 O7 P	1

Primary citation

CASK Functions as a Mg2+-independent neurexin kinase. Mukherjee, K., Sharma, M., Urlaub, H. et al. Cell (2008) 133:328-339. DOI 10.1016/j.cell.2008.02.036 · PubMed

Other PDB entries of the same protein (UniProt O14936 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1KGD 1.31 Å, Crystal Structure of the Guanylate Kinase-like Domain of Human CASK
9M6G 1.7 Å, the crystal structure of the Ca2+/CaM-CASK-CaMK-Mint1-CID complex
9KYS 1.76 Å, the Ca2+/CaM-CASK-ARD complex
9M5Y 1.8 Å, the crystal structure of the Ca2+/CaM-CASK-CaMK complex
6NH9 1.85 Å, Crystal structure of a human calcium/calmodulin dependent serine protein kinase (CASK)…
6NID 1.86 Å, Crystal structure of a human calcium/calmodulin dependent serine protein kinase (CASK)…
1KWA 1.93 Å, Human cask/lin-2 PDZ domain
7OAJ 1.93 Å, Crystal structure of pseudokinase CASK in complex with compound 7
3MFR 2.0 Å, CASK-4M CaM Kinase Domain, native
3MFS 2.1 Å, CASK-4M CaM Kinase Domain, AMPPNP
7OAL 2.17 Å, Crystal structure of pseudokinase CASK in complex with compound 25
3C0G 2.19 Å, CASK CaM-Kinase Domain- 3'-AMP complex, P1 form

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