6FEL: 14-3-3 gamma

Structure of 14-3-3 gamma in complex with CaMKK2 14-3-3 binding motif Ser511. Determined by X-ray diffraction at 2.84 Å resolution. Released 10 Jan 2018.

Method: X-ray diffraction
Resolution: 2.84 Å
Organism: Homo sapiens
Chains: 8
Atoms: 7,441
Mol. weight: 112.33 kDa
Released: 10 Jan 2018

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

Secondary structure: helices and β-sheets

6FEL contains 49 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: 12 helices, 0 β-strands

Element	Residues	Length
α-helix	4-16	13
α-helix	20-31	12
α-helix	39-73	35
α-helix	79-103	25
α-helix	104-108	5
α-helix	109-111	3
α-helix	117-137	21
α-helix	141-164	24
α-helix	170-185	16
α-helix	190-206	17
α-helix	208-210	3
α-helix	217-232	16

Chain B: 11 helices, 0 β-strands

Element	Residues	Length
α-helix	4-16	13
α-helix	20-31	12
α-helix	39-67	29
α-helix	78-103	26
α-helix	104-108	5
α-helix	117-135	19
α-helix	141-164	24
α-helix	170-185	16
α-helix	190-206	17
α-helix	208-210	3
α-helix	216-231	16

Chain C: 11 helices, 0 β-strands

Element	Residues	Length
α-helix	4-16	13
α-helix	20-31	12
α-helix	39-73	35
α-helix	78-103	26
α-helix	104-108	5
α-helix	117-135	19
α-helix	141-164	24
α-helix	170-181	12
α-helix	182-186	5
α-helix	190-205	16
α-helix	217-232	16

Chain D: 14 helices, 0 β-strands

Element	Residues	Length
α-helix	4-16	13
α-helix	20-31	12
α-helix	36-38	3
α-helix	39-68	30
α-helix	78-103	26
α-helix	104-108	5
α-helix	109-111	3
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 G: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	509-513	5

Molecules and chains

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

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

>6FEL_1 14-3-3 protein gamma (chains A, B, C, D)
GHMVDREQLVQKARLAEQAERYDDMAAAMKNVTELNEPLSNEERNLLSVAYKNVVGARRS
SWRVISSIEQKTSADGNEKKIEMVRAYREKIEKELEAVCQDVLSLLDNYLIKNCSETQYE
SKVFYLKMKGDYYRYLAEVATGEKRATVVESSEKAYSEAHEISKEHMQPTHPIRLGLALN
YSVFYYEIQNAPEQACHLAKTAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWT

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

>6FEL_2 Calcium/calmodulin-dependent protein kinase kinase 2 (chains E, F, G, H)
RSLSAPGN

Primary citation

14-3-3 protein directly interacts with the kinase domain of calcium/calmodulin-dependent protein kinase kinase (CaMKK2). Psenakova, K., Petrvalska, O., Kylarova, S. et al. Biochim Biophys Acta (2018) 1862:1612-1625. DOI 10.1016/j.bbagen.2018.04.006 · 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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