5D2D: Human 14-3-3 zeta

Crystal structure of human 14-3-3 zeta in complex with CFTR R-domain peptide pS753-pS768. Determined by X-ray diffraction at 2.1 Å resolution. Released 16 Mar 2016.

Method: X-ray diffraction
Resolution: 2.1 Å
Organism: Homo sapiens
Chains: 3
Atoms: 4,041
Mol. weight: 56.72 kDa
Released: 16 Mar 2016

Explore 5D2D in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5D2D contains 27 α-helices and 0 β-strands across 3 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: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	3-15	13
α-helix	19-31	13
α-helix	35-37	3
α-helix	38-67	30
α-helix	74-100	27
α-helix	101-105	5
α-helix	106-108	3
α-helix	112-132	21
α-helix	136-159	24
α-helix	165-176	12
α-helix	177-181	5
α-helix	185-200	16
α-helix	208-229	22

Chain B: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	3-15	13
α-helix	19-31	13
α-helix	35-37	3
α-helix	38-67	30
α-helix	75-100	26
α-helix	101-105	5
α-helix	106-108	3
α-helix	112-131	20
α-helix	138-159	22
α-helix	165-176	12
α-helix	177-181	5
α-helix	185-205	21
α-helix	214-227	14

Chain C: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	765-767	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
14-3-3 protein zeta/delta	A, B	protein	230	Homo sapiens	P63104 (AlphaFold model)
Cystic fibrosis transmembrane conductance regulator	C	protein	28	Homo sapiens	P13569 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>5D2D_1 14-3-3 protein zeta/delta (chains A, B)
MDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEERNLLSVAYKNVVGARRSSWR
VVSSIEQKTEGAEKKQQMAREYREKIETELRDICNDVLSLLEKFLIPNASQAESKVFYLK
MKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYE
ILNSPEKACSLAKTAFDEAIAELDTLSEESYKDSTLIMQLLRDNLTLWTS

Sequence of entity 2 (C), FASTA

>5D2D_2 Cystic fibrosis transmembrane conductance regulator (chains C)
AILPRISVISTGPTLQARRRQSVLNLMT

Primary citation

Characterization and small-molecule stabilization of the multisite tandem binding between 14-3-3 and the R domain of CFTR. Stevers, L.M., Lam, C.V., Leysen, S.F. et al. Proc Natl Acad Sci U S A (2016) 113:E1152-E1161. DOI 10.1073/pnas.1516631113 · PubMed

Other PDB entries of the same protein (UniProt P63104 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2O02 1.5 Å, Phosphorylation independent interactions between 14-3-3 and Exoenzyme S: from structure…
6F09 1.59 Å, Binary complex of 14-3-3 zeta with ubiquitin specific protease 8 (USP8) pSer718 peptide
7ZIT 1.79 Å, 14-3-3 in complex with SARS-COV2 N phospho-peptide
9UJ2 1.8 Å, 14-3-3 zeta chimera with the S202R peptide of SARS-CoV-2 N (residues 200-213)
6ZFG 1.85 Å, 14-3-3 zeta chimera with 18E6 and fusicoccin
6F08 1.9 Å, 14-3-3 zeta in complex with the human Son of sevenless homolog 1 (SOS1)
6ZFD 1.9 Å, 14-3-3 zeta bound to the phosphorylated 18E6 C-terminus
4FJ3 1.95 Å, 14-3-3 isoform zeta in complex with a diphoyphorylated C-RAF peptide
5EXA 1.95 Å, Small-molecule stabilization of the 14-3-3/Gab2 PPI interface
8P1H 1.95 Å, Crystal structure of the chimera of human 14-3-3 zeta and phosphorylated cytoplasmic…
8A9G 1.96 Å, Binary complex of 14-3-3 zeta Glucocorticoid Receptor (GR) pT524 peptide stabilised by…
1QJA 2.0 Å, 14-3-3 zeta/phosphopeptide complex (mode 2)

Browse structure collections

About this viewer

MolViewer shows 5D2D 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.