4J6S: 14-3-3gamma

14-3-3gamma complexed with the N-terminal sequence of tyrosine hydroxylase (residues 1-43). Determined by X-ray diffraction at 3.08 Å resolution. Released 2 Oct 2013.

Method: X-ray diffraction
Resolution: 3.08 Å
Organism: Homo sapiens
Chains: 8
Atoms: 7,970
Mol. weight: 136.1 kDa
Released: 2 Oct 2013

Explore 4J6S in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4J6S contains 50 α-helices and 0 β-strands across 5 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	4-16	13
α-helix	20-32	13
α-helix	36-38	3
α-helix	39-73	35
α-helix	76-103	28
α-helix	104-108	5
α-helix	117-137	21
α-helix	141-164	24
α-helix	170-182	13
α-helix	183-187	5
α-helix	190-206	17
α-helix	208-210	3
α-helix	213-233	21

Chain B: 12 helices, 0 β-strands

Element	Residues	Length
α-helix	4-16	13
α-helix	20-32	13
α-helix	36-38	3
α-helix	39-73	35
α-helix	76-103	28
α-helix	104-108	5
α-helix	117-137	21
α-helix	140-164	25
α-helix	170-185	16
α-helix	190-206	17
α-helix	208-210	3
α-helix	213-233	21

Chain C: 12 helices, 0 β-strands

Element	Residues	Length
α-helix	4-16	13
α-helix	20-32	13
α-helix	36-38	3
α-helix	39-72	34
α-helix	76-103	28
α-helix	104-108	5
α-helix	117-135	19
α-helix	140-164	25
α-helix	170-185	16
α-helix	190-206	17
α-helix	208-210	3
α-helix	213-233	21

Chain D: 12 helices, 0 β-strands

Element	Residues	Length
α-helix	4-16	13
α-helix	20-32	13
α-helix	36-38	3
α-helix	39-73	35
α-helix	76-103	28
α-helix	104-108	5
α-helix	117-135	19
α-helix	140-164	25
α-helix	170-185	16
α-helix	190-206	17
α-helix	208-210	3
α-helix	213-233	21

Chain G: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	503-505	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
14-3-3 protein gamma	A, B, C, D	protein	255	Homo sapiens	P61981 (AlphaFold model)
N-terminal motif of tyrosine hydroxylase	E, F, G, H	protein	43	Homo sapiens	P07101 (AlphaFold model)

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

>4J6S_1 14-3-3 protein gamma (chains A, B, C, D)
MSRRASVGLVDREQLVQKARLAEQAERYDDMAAAMKNVTELNEPLSNEERNLLSVAYKNV
VGARRSSWRVISSIEQKTSADGNEKKIEMVRAYREKIEKELEAVCQDVLSLLDNYLIKNC
SETQYESKVFYLKMKGDYYRYLAEVATGEKRATVVESSEKAYSEAHEISKEHMQPTHPIR
LGLALNYSVFYYEIQNAPEQACHLAKTAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTL
WTSDQQDDDGGEGNN

Sequence of entity 2 (E, F, G, H), FASTA

>4J6S_2 N-terminal motif of tyrosine hydroxylase (chains E, F, G, H)
MPTPDATTPQAKGFRRAVSELDAKQAEAIMSPRFIGRRQSLIE

Primary citation

The N-terminal sequence of tyrosine hydroxylase is a conformationally versatile motif that binds 14-3-3 proteins and membranes. Skjevik, A.A., Mileni, M., Baumann, A. et al. J Mol Biol (2014) 426:150-168. DOI 10.1016/j.jmb.2013.09.012 · PubMed

Other PDB entries of the same protein (UniProt P61981 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6S9K 1.6 Å, Structure of 14-3-3 gamma in complex with caspase-2 peptide containing 14-3-3 binding…
6ZBT 1.8 Å, Structure of 14-3-3 gamma in complex with Nedd4-2 14-3-3 binding motif Ser342
3UZD 1.86 Å, Crystal structure of 14-3-3 GAMMA
6ZC9 1.9 Å, Structure of 14-3-3 gamma in complex with Nedd4-2 14-3-3 binding motif Ser448
6A5S 2.1 Å, Structure of 14-3-3 gamma in complex with TFEB 14-3-3 binding motif
4E2E 2.25 Å, Crystal structure of a tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation…
7A6Y 2.5 Å, Structure of 14-3-3 gamma in complex with DAPK2 peptide stabilized by FC-A
2B05 2.55 Å, Crystal Structure of 14-3-3 gamma in complex with a phosphoserine peptide
6GKF 2.6 Å, Structure of 14-3-3 gamma in complex with caspase-2 14-3-3 binding motif Ser139
6BZD 2.67 Å, Structure of 14-3-3 gamma R57E mutant bound to GlcNAcylated peptide
7A6R 2.7 Å, Structure of 14-3-3 gamma in complex with DAPK2 peptide containing the 14-3-3 binding…
5D3E 2.75 Å, Crystal structure of human 14-3-3 gamma in complex with CFTR R-domain peptide pS768-pS795

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