6A5S: 14-3-3 gamma

Structure of 14-3-3 gamma in complex with TFEB 14-3-3 binding motif. Determined by X-ray diffraction at 2.1 Å resolution. Released 13 Feb 2019.

Method: X-ray diffraction
Resolution: 2.1 Å
Organism: Homo sapiens
Chains: 8
Atoms: 8,612
Mol. weight: 119.97 kDa
Ligands: MG
Released: 13 Feb 2019

Explore 6A5S in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6A5S 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 A: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	4-16	13
α-helix	20-32	13
α-helix	35-38	4
α-helix	39-69	31
α-helix	76-103	28
α-helix	104-108	5
α-helix	117-137	21
α-helix	140-164	25
α-helix	170-181	12
α-helix	182-186	5
α-helix	190-205	16
α-helix	208-210	3
α-helix	213-233	21

Chain B: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	4-16	13
α-helix	20-31	12
α-helix	35-38	4
α-helix	39-69	31
α-helix	76-103	28
α-helix	104-108	5
α-helix	117-137	21
α-helix	140-164	25
α-helix	170-181	12
α-helix	182-186	5
α-helix	190-205	16
α-helix	208-210	3
α-helix	213-233	21

Chain D: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	4-16	13
α-helix	20-32	13
α-helix	35-38	4
α-helix	39-68	30
α-helix	76-103	28
α-helix	104-108	5
α-helix	117-137	21
α-helix	140-164	25
α-helix	170-181	12
α-helix	182-186	5
α-helix	190-205	16
α-helix	208-210	3
α-helix	213-233	21

Chain G: 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	39-68	30
α-helix	77-103	27
α-helix	104-108	5
α-helix	117-137	21
α-helix	140-164	25
α-helix	170-181	12
α-helix	182-186	5
α-helix	190-205	16
α-helix	208-210	3
α-helix	213-233	21

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
14-3-3 protein gamma	A, B, D, G	protein	248	Homo sapiens	P61981 (AlphaFold model)
TFEB pS211-peptide	C, E, F, H	protein	15	Homo sapiens

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

>6A5S_1 14-3-3 protein gamma (chains A, B, D, G)
MVDREQLVQKARLAEQAERYDDMAAAMKNVTELNEPLSNEERNLLSVAYKNVVGARRSSW
RVISSIEQKTSADGNEKKIEMVRAYREKIEKELEAVCQDVLSLLDNYLIKNCSETQYESK
VFYLKMKGDYYRYLAEVATGEKRATVVESSEKAYSEAHEISKEHMQPTHPIRLGLALNYS
VFYYEIQNAPEQACHLAKTAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQQDD
DGGEGNNS

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

>6A5S_2 TFEB pS211-peptide (chains C, E, F, H)
LVGVTSSSCPADLTQ

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	1

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

Primary citation

YWHA/14-3-3 proteins recognize phosphorylated TFEB by a noncanonical mode for controlling TFEB cytoplasmic localization. Xu, Y., Ren, J., He, X. et al. Autophagy (2019) 15:1017-1030. DOI 10.1080/15548627.2019.1569928 · 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
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
6SAD 2.75 Å, Structure of 14-3-3 gamma in complex with double phosphorylated caspase-2 peptide on…

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