6Y4K: Human 14-3-3 gamma

Crystal structure of human 14-3-3 gamma in complex with CaMKK2 14-3-3 binding motif Ser100 and Fusicoccin A. Determined by X-ray diffraction at 3.0 Å resolution. Released 27 Jan 2021.

Method: X-ray diffraction
Resolution: 3.0 Å
Organism: Homo sapiens
Chains: 4
Atoms: 3,530
Mol. weight: 57.3 kDa
Ligands: FSC
Released: 27 Jan 2021

Explore 6Y4K in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6Y4K contains 22 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: 11 helices, 0 β-strands

Element	Residues	Length
α-helix	4-16	13
α-helix	20-32	13
α-helix	36-38	3
α-helix	39-69	31
α-helix	78-106	29
α-helix	117-135	19
α-helix	141-164	24
α-helix	170-185	16
α-helix	190-205	16
α-helix	208-210	3
α-helix	216-231	16

Chain B: 11 helices, 0 β-strands

Element	Residues	Length
α-helix	4-14	11
α-helix	15-17	3
α-helix	20-31	12
α-helix	39-68	30
α-helix	79-103	25
α-helix	104-108	5
α-helix	117-135	19
α-helix	140-163	24
α-helix	170-185	16
α-helix	190-204	15
α-helix	220-233	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
14-3-3 protein gamma	A, B	protein	236	Homo sapiens	P61981 (AlphaFold model)
Calcium/calmodulin-dependent protein kinase kinase 2	E, F	protein	8	Homo sapiens	Q96RR4 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>6Y4K_1 14-3-3 protein gamma (chains A, B)
GHMVDREQLVQKARLAEQAERYDDMAAAMKNVTELNEPLSNEERNLLSVAYKNVVGARRS
SWRVISSIEQKTSADGNEKKIEMVRAYREKIEKELEAVCQDVLSLLDNYLIKNCSETQYE
SKVFYLKMKGDYYRYLAEVATGEKRATVVESSEKAYSEAHEISKEHMQPTHPIRLGLALN
YSVFYYEIQNAPEQACHLAKTAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWT

Sequence of entity 2 (E, F), FASTA

>6Y4K_2 Calcium/calmodulin-dependent protein kinase kinase 2 (chains E, F)
RKLSLQER

Ligands and cofactors

ID	Name	Formula	Copies
FSC	Fusicoccin	C36 H56 O12	1

Primary citation

Stabilization of Protein-Protein Interactions between CaMKK2 and 14-3-3 by Fusicoccins. Lentini Santo, D., Petrvalska, O., Obsilova, V. et al. ACS Chem Biol (2020) 15:3060-3071. DOI 10.1021/acschembio.0c00821 · 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

Browse structure collections

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