7QI1: Human 14-3-3 protein beta

Crystal structure of human 14-3-3 protein beta in complex with CFTR peptide pS753pS768 and PPI stabilizer CY007424. Determined by X-ray diffraction at 1.76 Å resolution. Released 25 May 2022.

Method: X-ray diffraction
Resolution: 1.76 Å
Organism: Homo sapiens
Chains: 6
Atoms: 8,367
Mol. weight: 116.44 kDa
Ligands: GLN, TYR, Q95, ARG
Released: 25 May 2022

Explore 7QI1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7QI1 contains 56 α-helices and 2 β-strands across 6 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, 0 β-strands

Element	Residues	Length
α-helix	5-17	13
α-helix	21-33	13
α-helix	36-39	4
α-helix	40-69	30
α-helix	75-102	28
α-helix	103-107	5
α-helix	108-110	3
α-helix	114-134	21
α-helix	137-161	25
α-helix	167-178	12
α-helix	179-183	5
α-helix	187-205	19
α-helix	210-212	3
α-helix	214-230	17

Chain B: 14 helices, 0 β-strands

Element	Residues	Length
α-helix	0-2	3
α-helix	5-17	13
α-helix	21-33	13
α-helix	36-39	4
α-helix	40-68	29
α-helix	75-102	28
α-helix	103-107	5
α-helix	108-110	3
α-helix	114-134	21
α-helix	137-161	25
α-helix	167-178	12
α-helix	179-183	5
α-helix	187-202	16
α-helix	210-230	21

Chain C: 13 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	5-17	13
α-helix	21-33	13
α-helix	37-39	3
α-helix	40-70	31
α-helix	75-102	28
α-helix	103-107	5
α-helix	114-134	21
α-helix	137-161	25
α-helix	167-178	12
α-helix	179-183	5
α-helix	187-205	19
β-strand	208	1	1
α-helix	210-213	4
α-helix	214-230	17

Chain D: 14 helices, 0 β-strands

Element	Residues	Length
α-helix	0-2	3
α-helix	5-17	13
α-helix	21-33	13
α-helix	37-39	3
α-helix	40-69	30
α-helix	75-102	28
α-helix	103-107	5
α-helix	114-132	19
α-helix	137-161	25
α-helix	167-178	12
α-helix	179-183	5
α-helix	187-202	16
α-helix	207-213	7
α-helix	214-231	18

Chain E: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	769	1	1

Chain F: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	753-756	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
14-3-3 protein theta	A, B, C, D	protein	237	Homo sapiens	S7N159 (AlphaFold model)
Cystic fibrosis transmembrane conductance regulator	E, F	protein	28	Homo sapiens	P13569 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>7QI1_1 14-3-3 protein theta (chains A, B, C, D)
GAMGSMTMDKSELVQKAKLAEQAERYDDMAAAMKAVTEQGHELSNEERNLLSVAYKNVVG
ARRSSWRVISSIEQKTERNEKKQQMGKEYREKIEAELQDICNDVLELLDKYLIPNATQPE
SKVFYLKMKGDYFRYLSEVASGDNKQTTVSNSQQAYQEAFEISKKEMQPTHPIRLGLALN
FSVFYYEILNSPEKACSLAKTAFDEAIAELDTLNEESYKDSTLIMQLLRDNLTLWTS

Sequence of entity 2 (E, F), FASTA

>7QI1_2 Cystic fibrosis transmembrane conductance regulator (chains E, F)
AILPRISVISTGPTLQARRRQSVLNLMT

Ligands and cofactors

ID	Name	Formula	Copies
GLN	Glutamine	C5 H10 N2 O3	2
TYR	Tyrosine	C9 H11 N O3	2
Q95	[2-(2-methylphenyl)sulfanylphenyl]methanamine	C14 H15 N S	2
ARG	Arginine	C6 H15 N4 O2	2

Primary citation

Macrocycle-stabilization of its interaction with 14-3-3 increases plasma membrane localization and activity of CFTR. Stevers, L.M., Wolter, M., Carlile, G.W. et al. Nat Commun (2022) 13:3586-3586. DOI 10.1038/s41467-022-31206-6 · PubMed

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