4ZDR: 14-3-3[zeta]-LKB1 fusion protein

Crystal structure of 14-3-3[zeta]-LKB1 fusion protein. Determined by X-ray diffraction at 2.9 Å resolution. Released 9 Sept 2015.

Method: X-ray diffraction
Resolution: 2.9 Å
Organisms: Homo sapiens, synthetic construct
Chains: 2
Atoms: 3,754
Mol. weight: 61.43 kDa
Ligands: TME
Released: 9 Sept 2015

Explore 4ZDR in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4ZDR contains 27 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	0-2	3
α-helix	3-15	13
α-helix	19-31	13
α-helix	34-37	4
α-helix	38-67	30
α-helix	74-100	27
α-helix	101-105	5
α-helix	112-132	21
α-helix	135-159	25
α-helix	165-176	12
α-helix	177-181	5
α-helix	185-200	16
α-helix	208-227	20
α-helix	238-240	3

Chain B: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	3-15	13
α-helix	19-31	13
α-helix	35-36	2
α-helix	38-67	30
α-helix	75-100	26
α-helix	101-105	5
α-helix	106-108	3
α-helix	112-130	19
α-helix	135-159	25
α-helix	165-176	12
α-helix	177-181	5
α-helix	185-201	17
α-helix	212-229	18

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
14-3-3 protein zeta/delta,GGSGGS linker,Serine/threonine-protein kinase STK11	A, B	protein	266	Homo sapiens, synthetic construct	P63104 (AlphaFold model), Q15831 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4ZDR_1 14-3-3 protein zeta/delta,GGSGGS linker,Serine/threonine-protein kinase STK11 (chains A, B)
MSYYHHHHHHLESTSLYKKAGLMDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSN
EERNLLSVAYKNVVGARRSSWRVVSSIEQKTEGAEKKQQMAREYREKIETELRDICNDVL
SLLEKFLIPNASQAESKVFYLKMKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISKK
EMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLSEESYKDSTLIM
QLLRDNLTLWTSGGSGGSRSMEVVPY

Ligands and cofactors

ID	Name	Formula	Copies
TME	Propane	C3 H8	6

Water and common crystallization additives (SO4, GOL) are not listed.

Primary citation

Structure of the 14-3-3 zeta-LKB1 fusion protein provides insight into a novel ligand-binding mode of 14-3-3. Ding, S., Zhou, R., Zhu, Y. Acta Crystallogr F Struct Biol Commun (2015) 71:1114-1119. DOI 10.1107/S2053230X15012595 · PubMed

Other PDB entries of the same protein (UniProt P63104 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2O02 1.5 Å, Phosphorylation independent interactions between 14-3-3 and Exoenzyme S: from structure…
6F09 1.59 Å, Binary complex of 14-3-3 zeta with ubiquitin specific protease 8 (USP8) pSer718 peptide
7ZIT 1.79 Å, 14-3-3 in complex with SARS-COV2 N phospho-peptide
9UJ2 1.8 Å, 14-3-3 zeta chimera with the S202R peptide of SARS-CoV-2 N (residues 200-213)
6ZFG 1.85 Å, 14-3-3 zeta chimera with 18E6 and fusicoccin
6F08 1.9 Å, 14-3-3 zeta in complex with the human Son of sevenless homolog 1 (SOS1)
6ZFD 1.9 Å, 14-3-3 zeta bound to the phosphorylated 18E6 C-terminus
4FJ3 1.95 Å, 14-3-3 isoform zeta in complex with a diphoyphorylated C-RAF peptide
5EXA 1.95 Å, Small-molecule stabilization of the 14-3-3/Gab2 PPI interface
8P1H 1.95 Å, Crystal structure of the chimera of human 14-3-3 zeta and phosphorylated cytoplasmic…
8A9G 1.96 Å, Binary complex of 14-3-3 zeta Glucocorticoid Receptor (GR) pT524 peptide stabilised by…
1QJA 2.0 Å, 14-3-3 zeta/phosphopeptide complex (mode 2)

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