6F09: 14-3-3 protein zeta/delta

Binary complex of 14-3-3 zeta with ubiquitin specific protease 8 (USP8) pSer718 peptide. Determined by X-ray diffraction at 1.59 Å resolution. Released 7 Mar 2018.

Method: X-ray diffraction
Resolution: 1.59 Å
Organism: Homo sapiens
Chains: 8
Atoms: 7,997
Mol. weight: 111.69 kDa
Released: 7 Mar 2018

Explore 6F09 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6F09 contains 52 α-helices and 0 β-strands across 4 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 P: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	3-15	13
α-helix	19-30	12
α-helix	38-68	31
α-helix	73-100	28
α-helix	101-105	5
α-helix	106-108	3
α-helix	112-132	21
α-helix	138-159	22
α-helix	165-176	12
α-helix	177-181	5
α-helix	185-200	16
α-helix	203-205	3
α-helix	208-228	21

Chain Q: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	3-15	13
α-helix	19-31	13
α-helix	34-37	4
α-helix	38-68	31
α-helix	77-100	24
α-helix	101-105	5
α-helix	112-132	21
α-helix	138-159	22
α-helix	165-176	12
α-helix	177-181	5
α-helix	185-201	17
α-helix	203-205	3
α-helix	211-228	18

Chain R: 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	38-68	31
α-helix	73-100	28
α-helix	101-105	5
α-helix	106-108	3
α-helix	112-130	19
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 S: 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	38-68	31
α-helix	73-100	28
α-helix	101-105	5
α-helix	106-108	3
α-helix	112-132	21
α-helix	138-159	22
α-helix	165-176	12
α-helix	177-181	5
α-helix	185-204	20
α-helix	214-228	15

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
14-3-3 protein zeta/delta	P, Q, R, S	protein	230	Homo sapiens	P63104 (AlphaFold model)
Ubiquitin carboxyl-terminal hydrolase 8	A, B, C, D	protein	13	Homo sapiens	P40818 (AlphaFold model)

Sequence of entity 1 (P, Q, R, S), FASTA

>6F09_1 14-3-3 protein zeta/delta (chains P, Q, R, S)
MDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEERNLLSVAYKNVVGARRSSWR
VVSSIEQKTEGAEKKQQMAREYREKIETELRDICNDVLSLLEKFLIPNASQAESKVFYLK
MKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYE
ILNSPEKACSLAKTAFDEAIAELDTLSEESYKDSTLIMQLLRDNLTLWTS

Sequence of entity 2 (A, B, C, D), FASTA

>6F09_2 Ubiquitin carboxyl-terminal hydrolase 8 (chains A, B, C, D)
KLKRSYSSPDITQ

Primary citation

Biophysical and structural insight into the USP8/14-3-3 interaction. Centorrino, F., Ballone, A., Wolter, M. et al. FEBS Lett (2018) 592:1211-1220. DOI 10.1002/1873-3468.13017 · 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…
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)
1QJB 2.0 Å, 14-3-3 zeta/phosphopeptide complex (mode 1)

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