2O02: 14-3-3 protein zeta/delta

Phosphorylation independent interactions between 14-3-3 and Exoenzyme S: from structure to pathogenesis. Determined by X-ray diffraction at 1.5 Å resolution. Released 27 Nov 2007.

Method: X-ray diffraction
Resolution: 1.5 Å
Organism: Homo sapiens
Chains: 4
Atoms: 4,882
Mol. weight: 55.61 kDa
Ligands: BEZ
Released: 27 Nov 2007

Explore 2O02 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2O02 contains 30 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 A: 14 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	76-100	25
α-helix	101-105	5
α-helix	106-108	3
α-helix	112-131	20
α-helix	135-159	25
α-helix	165-176	12
α-helix	177-181	5
α-helix	185-200	16
α-helix	203-205	3
α-helix	211-228	18

Chain B: 14 helices, 0 β-strands

Element	Residues	Length
α-helix	3-15	13
α-helix	19-32	14
α-helix	35-37	3
α-helix	38-68	31
α-helix	73-100	28
α-helix	101-105	5
α-helix	112-131	20
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	208-210	3
α-helix	211-228	18

Chains P and Q: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	422-425	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
14-3-3 protein zeta/delta	A, B	protein	230	Homo sapiens	P63104 (AlphaFold model)
ExoS (416-430) peptide	P, Q	protein	14

Sequence of entity 1 (A, B), FASTA

>2O02_1 14-3-3 protein zeta/delta (chains A, B)
MDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEERNLLSVAYKNVVGARRSSWR
VVSSIEQKTEGAEKKQQMAREYREKIETELRDICNDVLSLLEKFLIPNASQAESKVFYLK
MKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYE
ILNSPEKACSLAKTAFDEAIAELDTLSEESYKDSTLIMQLLRDNLTLWTS

Sequence of entity 2 (P, Q), FASTA

>2O02_2 ExoS (416-430) peptide (chains P, Q)
GHGQGLLDALDLAS

Ligands and cofactors

ID	Name	Formula	Copies
BEZ	Benzoic acid	C7 H6 O2	2

Primary citation

Phosphorylation-independent interaction between 14-3-3 and exoenzyme S: from structure to pathogenesis. Ottmann, C., Yasmin, L., Weyand, M. et al. EMBO J (2007) 26:902-913. DOI 10.1038/sj.emboj.7601530 · PubMed

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

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)
1QJB 2.0 Å, 14-3-3 zeta/phosphopeptide complex (mode 1)

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