6ZBT: 14-3-3 gamma

Structure of 14-3-3 gamma in complex with Nedd4-2 14-3-3 binding motif Ser342. Determined by X-ray diffraction at 1.8 Å resolution. Released 21 Jul 2021.

Method: X-ray diffraction
Resolution: 1.8 Å
Organism: Homo sapiens
Chains: 8
Atoms: 8,014
Mol. weight: 113.21 kDa
Ligands: CFH
Released: 21 Jul 2021

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

Secondary structure: helices and β-sheets

6ZBT 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	20-31	12
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	170-181	12
α-helix	182-186	5
α-helix	190-205	16
α-helix	208-210	3
α-helix	216-233	18

Chain B: 12 helices, 0 β-strands

Element	Residues	Length
α-helix	4-16	13
α-helix	20-31	12
α-helix	36-38	3
α-helix	39-69	31
α-helix	77-103	27
α-helix	104-108	5
α-helix	117-136	20
α-helix	140-164	25
α-helix	170-181	12
α-helix	182-186	5
α-helix	190-205	16
α-helix	213-233	21

Chain C: 14 helices, 0 β-strands

Element	Residues	Length
α-helix	5-16	12
α-helix	20-31	12
α-helix	36-38	3
α-helix	39-68	30
α-helix	78-103	26
α-helix	104-108	5
α-helix	117-137	21
α-helix	140-142	3
α-helix	143-164	22
α-helix	170-181	12
α-helix	182-186	5
α-helix	190-206	17
α-helix	208-210	3
α-helix	216-233	18

Chain D: 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	76-103	28
α-helix	104-108	5
α-helix	117-136	20
α-helix	140-164	25
α-helix	170-181	12
α-helix	182-187	6
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, C, D	protein	234	Homo sapiens	P61981 (AlphaFold model)
E3 ubiquitin-protein ligase NEDD4-like	E, F, G, H	protein	10	Homo sapiens	Q96PU5 (AlphaFold model)

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

>6ZBT_1 14-3-3 protein gamma (chains A, B, C, D)
MVDREQLVQKARLAEQAERYDDMAAAMKNVTELNEPLSNEERNLLSVAYKNVVGARRSSW
RVISSIEQKTSADGNEKKIEMVRAYREKIEKELEAVCQDVLSLLDNYLIKNCSETQYESK
VFYLKMKGDYYRYLAEVATGEKRATVVESSEKAYSEAHEISKEHMQPTHPIRLGLALNYS
VFYYEIQNAPEQACHLAKTAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWT

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

>6ZBT_2 E3 ubiquitin-protein ligase NEDD4-like (chains E, F, G, H)
LRSCSVTDAV

Ligands and cofactors

ID	Name	Formula	Copies
CFH	1,1,1,3,3,3-hexafluoropropan-2-ol	C3 H2 F6 O	4

Primary citation

14-3-3-protein regulates Nedd4-2 by modulating interactions between HECT and WW domains. Pohl, P., Joshi, R., Petrvalska, O. et al. Commun Biol (2021) 4:899-899. DOI 10.1038/s42003-021-02419-0 · 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…
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
6SAD 2.75 Å, Structure of 14-3-3 gamma in complex with double phosphorylated caspase-2 peptide on…

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