9CKX: Dsk2 Sti1 domain

Crystal structure of Dsk2 Sti1 domain bound to a transmembrane domain. Determined by X-ray diffraction at 1.98 Å resolution. Released 12 Mar 2025.

Method: X-ray diffraction
Resolution: 1.98 Å
Organisms: Metschnikowia bicuspidata, Myxococcus xanthus, Homo sapiens
Chains: 2
Atoms: 3,516
Mol. weight: 48.84 kDa
Released: 12 Mar 2025

Explore 9CKX in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9CKX contains 28 α-helices and 14 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: 14 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	5-12	8
α-helix	14-25	12
α-helix	27-35	9
α-helix	45-49	5
α-helix	51-60	10
α-helix	63-75	13
β-strand	79-83	5	1
α-helix	87-100	14
β-strand	103-107	5	1
α-helix	110-120	11
β-strand	124-128	5	1
β-strand	130	1	2
β-strand	136	1	2
α-helix	137-146	10
β-strand	155-159	5	1
α-helix	161-163	3
α-helix	164-168	5
β-strand	176-179	4	1
α-helix	182	1
α-helix	184-194	11
α-helix	198-221	24

Chain B: 14 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	5-12	8
α-helix	14-25	12
α-helix	27-36	10
α-helix	45-49	5
α-helix	51-60	10
α-helix	63-75	13
β-strand	79-83	5	3
α-helix	87-100	14
β-strand	103-107	5	3
α-helix	110-120	11
β-strand	124-128	5	3
β-strand	130	1	4
β-strand	136	1	4
α-helix	137-146	10
β-strand	155-159	5	3
α-helix	161-163	3
α-helix	164-169	6
β-strand	176-179	4	3
α-helix	182	1
α-helix	184-194	11
α-helix	198-221	24

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ubiquitin-domain-containing protein,Response regulator FrzS,Vesicle-associated membrane protein 2	A, B	protein	222	Metschnikowia bicuspidata, Myxococcus xanthus, Homo sapiens	P63027 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>9CKX_1 Ubiquitin-domain-containing protein,Response regulator FrzS,Vesicle-associated membrane protein 2 (chains A, B)
GPHMEQLEGIMLSPAFQEQMNALMLDPRMLDMMIDQNPQLRNMGPEARQMLRPMFREMMS
NPESMRSMMNMGRAWGSKKILIVESDTALSATLRSALEGRGFTVDETTDGKGSVEQIRRD
RPDLVVLAVDLSAGQNGYLICGKLKKDDDLKNVPIVIIGNPDGFAQHRKLKAHADEYVAK
PVDADQLVERAGALIGFPEGNSMMIALGVACAIALAIAAVYF

Primary citation

ALS mutations disrupt self-association between the Ubiquilin Sti1 hydrophobic groove and internal placeholder sequences. Onwunma, J., Binsabaan, S., Allen, S.P. et al. bioRxiv (2025). DOI 10.1101/2024.07.10.602902 · PubMed

Other PDB entries of the same protein (UniProt P63027 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3FIE 2.1 Å, Crystal structure of Clostridium botulinum neurotoxin serotype F catalytic domain with…
3FII 2.17 Å, Crystal structure of Clostridium botulinum neurotoxin serotype F catalytic domain with…
3RK2 2.2 Å, Truncated SNARE complex
3RK3 3.5 Å, Truncated SNARE complex with complexin
7UDC 3.7 Å, cryo-EM structures of a synaptobrevin-Munc18-1-syntaxin-1 complex class1
3RL0 3.8 Å, Truncated SNARE complex with complexin (P1)

Browse structure collections

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