3UZD: 14-3-3 GAMMA

Crystal structure of 14-3-3 GAMMA. Determined by X-ray diffraction at 1.86 Å resolution. Released 21 Mar 2012.

Method: X-ray diffraction
Resolution: 1.86 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,023
Mol. weight: 30.51 kDa
Ligands: MG
Released: 21 Mar 2012

Explore 3UZD in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3UZD contains 15 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: 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	39-70	32
α-helix	79-103	25
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	190-206	17
α-helix	208-210	3
α-helix	216-233	18

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	9-13	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
14-3-3 protein gamma	A	protein	248	Homo sapiens	P61981 (AlphaFold model)
Histone deacetylase 4	B	protein	17	Homo sapiens	P56524 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3UZD_1 14-3-3 protein gamma (chains A)
MVDREQLVQKARLAEQAERYDDMAAAMKNVTELNEPLSNEERNLLSVAYKNVVGARRSSW
RVISSIEQKTSADGNEKKIEMVRAYREKIEKELEAVCQDVLSLLDNYLIKNCSETQYESK
VFYLKMKGDYYRYLAEVATGEKRATVVESSEKAYSEAHEISKEHMQPTHPIRLGLALNYS
VFYYEIQNAPEQACHLAKTAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQQDD
DGGEGNNS

Sequence of entity 2 (B), FASTA

>3UZD_2 Histone deacetylase 4 (chains B)
LPLYTSPSLPNITLGLP

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	1

Water and common crystallization additives (NO3) are not listed.

Primary citation

Sequence-Specific Recognition of a PxLPxI/L Motif by an Ankyrin Repeat Tumbler Lock. Xu, C., Jin, J., Bian, C. et al. Sci Signal (2012) 5:ra39-ra39. DOI 10.1126/scisignal.2002979 · 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
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…

Browse structure collections

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