2C1N: 14-3-3 protein zeta/delta

Molecular basis for the recognition of phosphorylated and phosphoacetylated histone H3 by 14-3-3. Determined by X-ray diffraction at 2.0 Å resolution. Released 2 Nov 2005.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: HOMO SAPIENS
Chains: 4
Atoms: 3,972
Mol. weight: 60.37 kDa
Released: 2 Nov 2005

Explore 2C1N in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2C1N contains 23 α-helices and 0 β-strands across 2 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: 12 helices, 0 β-strands

Element	Residues	Length
α-helix	3-15	13
α-helix	19-30	12
α-helix	35-37	3
α-helix	38-68	31
α-helix	73-100	28
α-helix	101-105	5
α-helix	112-130	19
α-helix	142-159	18
α-helix	165-180	16
α-helix	185-200	16
α-helix	203-205	3
α-helix	211-227	17

Chain B: 11 helices, 0 β-strands

Element	Residues	Length
α-helix	3-16	14
α-helix	19-30	12
α-helix	35-37	3
α-helix	38-68	31
α-helix	73-100	28
α-helix	101-105	5
α-helix	112-130	19
α-helix	142-159	18
α-helix	165-180	16
α-helix	185-200	16
α-helix	211-227	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
14-3-3 protein zeta/delta	A, B	protein	258	HOMO SAPIENS	P63104 (AlphaFold model)
Histone H3 acetylphosphopeptide	C, E	protein	8	HOMO SAPIENS	P68431 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>2C1N_1 14-3-3 PROTEIN ZETA/DELTA (chains A, B)
MGSSHHHHHHSQDMDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEERNLLSVA
YKNVVGARRSSWRVVSSIEQKTEGAEKKQQMAREYREKIETELRDICNDVLSLLEKFLIP
NASQAESKVFYLKMKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISKKEMQPTHPIR
LGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLSEESYKDSTLIMQLLRDNLTL
WTSDTQGDEAEAGEGGEN

Sequence of entity 2 (C, E), FASTA

>2C1N_2 HISTONE H3 ACETYLPHOSPHOPEPTIDE (chains C, E)
ARKSTGGK

Primary citation

Molecular Basis for the Recognition of Phosphorylated and Phosphoacetylated Histone H3 by 14-3-3. Macdonald, N., Welburn, J.P.I., Noble, M.E.M. et al. Mol Cell (2005) 20:199. DOI 10.1016/J.MOLCEL.2005.08.032 · 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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