2WH0: 14-3-3 protein zeta/delta

Recognition of an intrachain tandem 14-3-3 binding site within protein kinase C epsilon. Determined by X-ray diffraction at 2.25 Å resolution. Released 18 Aug 2009.

Method: X-ray diffraction
Resolution: 2.25 Å
Organism: HOMO SAPIENS
Chains: 6
Atoms: 6,877
Mol. weight: 118.76 kDa
Ligands: CA
Released: 18 Aug 2009

Explore 2WH0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2WH0 contains 49 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: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	3-15	13
α-helix	19-31	13
α-helix	35-36	2
α-helix	38-67	30
α-helix	73-100	28
α-helix	101-105	5
α-helix	106-108	3
α-helix	112-131	20
α-helix	136-157	22
α-helix	165-176	12
α-helix	177-182	6
α-helix	185-202	18
α-helix	211-228	18

Chain B: 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	38-68	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	211-227	17

Chain C: 11 helices, 0 β-strands

Element	Residues	Length
α-helix	5-15	11
α-helix	19-30	12
α-helix	38-67	30
α-helix	73-100	28
α-helix	101-105	5
α-helix	112-130	19
α-helix	136-159	24
α-helix	165-176	12
α-helix	177-181	5
α-helix	185-201	17
α-helix	211-228	18

Chain D: 11 helices, 0 β-strands

Element	Residues	Length
α-helix	4-15	12
α-helix	19-32	14
α-helix	35-36	2
α-helix	38-65	28
α-helix	73-100	28
α-helix	101-105	5
α-helix	112-130	19
α-helix	138-159	22
α-helix	165-180	16
α-helix	185-201	17
α-helix	211-227	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
14-3-3 protein zeta/delta	A, B, C, D	protein	245	HOMO SAPIENS	P63104 (AlphaFold model)
Protein kinase C epsilon type, npkc-epsilon	Q, R	protein	31	HOMO SAPIENS	Q02156 (AlphaFold model)

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

>2WH0_1 14-3-3 PROTEIN ZETA/DELTA (chains A, B, C, D)
MDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEERNLLSVAYKNVVGARRSSWR
VVSSIEQKTEGAEKKQQMAREYREKIETELRDICNDVLSLLEKFLIPNASQAESKVFYLK
MKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYE
ILNSPEKACSLAKTAFDEAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDTQGDEAEAG
EGGEN

Sequence of entity 2 (Q, R), FASTA

>2WH0_2 PROTEIN KINASE C EPSILON TYPE, NPKC-EPSILON (chains Q, R)
DRSKSAPTSPCDQEIKELENNIRKALSFDNR

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	1

Water and common crystallization additives (PGE) are not listed.

Primary citation

Recognition of an Intra-Chain Tandem 14-3-3 Binding Site within Pkc Epsilon. Kostelecky, B., Saurin, A.T., Purkiss, A. et al. EMBO Rep (2009) 10:983. DOI 10.1038/EMBOR.2009.150 · 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)

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