6F08: 14-3-3 zeta

14-3-3 zeta in complex with the human Son of sevenless homolog 1 (SOS1). Determined by X-ray diffraction at 1.9 Å resolution. Released 14 Feb 2018.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Homo sapiens
Chains: 8
Atoms: 7,819
Mol. weight: 111.6 kDa
Released: 14 Feb 2018

Explore 6F08 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6F08 contains 53 α-helices and 0 β-strands across 8 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	3-16	14
α-helix	19-31	13
α-helix	35-37	3
α-helix	38-66	29
α-helix	76-100	25
α-helix	101-105	5
α-helix	106-108	3
α-helix	119-132	14
α-helix	138-159	22
α-helix	165-180	16
α-helix	185-201	17
α-helix	203-205	3
α-helix	211-228	18

Chain B: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	4-15	12
α-helix	19-31	13
α-helix	38-67	30
α-helix	73-100	28
α-helix	101-105	5
α-helix	112-132	21
α-helix	138-159	22
α-helix	165-180	16
α-helix	185-202	18
α-helix	214-228	15

Chains D, K, N and Q: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	4-6	3

Chain I: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	3-16	14
α-helix	19-31	13
α-helix	35-37	3
α-helix	38-67	30
α-helix	76-100	25
α-helix	101-105	5
α-helix	112-132	21
α-helix	141-159	19
α-helix	165-176	12
α-helix	177-181	5
α-helix	185-201	17
α-helix	203-205	3
α-helix	211-229	19

Chain J: 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	38-66	29
α-helix	75-100	26
α-helix	101-105	5
α-helix	106-108	3
α-helix	112-130	19
α-helix	141-159	19
α-helix	165-176	12
α-helix	177-181	5
α-helix	185-201	17
α-helix	212-228	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
14-3-3 protein zeta/delta	A, B, I, J	protein	230	Homo sapiens	P63104 (AlphaFold model)
Son of sevenless homolog 1	D, K, N, Q	protein	13	Homo sapiens	Q07889 (AlphaFold model)

Sequence of entity 1 (A, B, I, J), FASTA

>6F08_1 14-3-3 protein zeta/delta (chains A, B, I, J)
MDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEERNLLSVAYKNVVGARRSSWR
VVSSIEQKTEGAEKKQQMAREYREKIETELRDICNDVLSLLEKFLIPNASQAESKVFYLK
MKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYE
ILNSPEKACSLAKTAFDEAIAELDTLSEESYKDSTLIMQLLRDNLTLWTS

Sequence of entity 2 (D, K, N, Q), FASTA

>6F08_2 Son of sevenless homolog 1 (chains D, K, N, Q)
PRRRPESAPAESS

Primary citation

Structural characterization of 14-3-3 zeta in complex with the human Son of sevenless homolog 1 (SOS1). Ballone, A., Centorrino, F., Wolter, M. et al. J Struct Biol (2018) 202:210-215. DOI 10.1016/j.jsb.2018.01.011 · 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
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)
1QJB 2.0 Å, 14-3-3 zeta/phosphopeptide complex (mode 1)

Browse structure collections

About this viewer

MolViewer shows 6F08 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.