3C0G: CASK CaM-Kinase Domain- 3'-AMP complex, P1 form

CASK CaM-Kinase Domain- 3'-AMP complex, P1 form. Determined by X-ray diffraction at 2.19 Å resolution. Released 29 Apr 2008.

Method: X-ray diffraction
Resolution: 2.19 Å
Organism: Homo sapiens
Chains: 2
Atoms: 5,363
Mol. weight: 79.21 kDa
Ligands: 3AM
Released: 29 Apr 2008

Explore 3C0G in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3C0G contains 38 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: 19 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	45-50	6
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
β-strand	98	1	2
α-helix	99-109	11
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	174-175	2	4
α-helix	188-191	4
β-strand	196-197	2	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	267-270	4
α-helix	274-277	4
α-helix	279-282	4
α-helix	289-302	14
α-helix	309-312	4

Chain B: 19 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	8-10	3
β-strand	12-20	9	5
β-strand	24-31	8	5
β-strand	37-44	8	5
α-helix	45-50	6
α-helix	56-68	13
β-strand	74	1	6
β-strand	77-83	7	5
β-strand	86-92	7	5
β-strand	98	1	6
α-helix	99-108	10
α-helix	115-134	20
β-strand	137-138	2	7
α-helix	144-146	3
β-strand	147-149	3	6
α-helix	156-157	2
β-strand	158-160	3	6
β-strand	167-168	2	7
β-strand	174-175	2	8
α-helix	183-185	3
α-helix	188-191	4
β-strand	196-197	2	8
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	267-270	4
α-helix	274-277	4
α-helix	279-282	4
α-helix	289-302	14
α-helix	306-312	7

Molecules and chains

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

Sequence of entity 1 (A, B), FASTA

>3C0G_1 Peripheral plasma membrane protein CASK (chains A, B)
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	2

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
3C0I 1.85 Å, CASK CaM-Kinase Domain- 3'-AMP complex, P212121 form
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

Browse structure collections

About this viewer

MolViewer shows 3C0G directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.