8A9G: 14-3-3 protein zeta/delta

Binary complex of 14-3-3 zeta Glucocorticoid Receptor (GR) pT524 peptide stabilised by (R)-para chloropyrrolidone1. Determined by X-ray diffraction at 1.96 Å resolution. Released 28 Dec 2022.

Method: X-ray diffraction
Resolution: 1.96 Å
Organism: Homo sapiens
Chains: 4
Atoms: 4,269
Mol. weight: 57.79 kDa
Ligands: QJK, MG, BTB
Released: 28 Dec 2022

Explore 8A9G in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8A9G contains 29 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	3-15	13
α-helix	19-31	13
α-helix	35-37	3
α-helix	38-68	31
α-helix	74-100	27
α-helix	101-105	5
α-helix	112-131	20
α-helix	138-159	22
α-helix	165-176	12
α-helix	177-181	5
α-helix	185-201	17
α-helix	203-205	3
α-helix	211-228	18

Chain B: 12 helices, 0 β-strands

Element	Residues	Length
α-helix	2-15	14
α-helix	19-30	12
α-helix	35-37	3
α-helix	38-67	30
α-helix	73-100	28
α-helix	101-105	5
α-helix	112-131	20
α-helix	135-159	25
α-helix	165-180	16
α-helix	185-201	17
α-helix	203-205	3
α-helix	211-229	19

Chain C: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	520-523	4
α-helix	527-529	3

Chain D: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	521-523	3
α-helix	527-529	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
14-3-3 protein zeta/delta	A, B	protein	235	Homo sapiens	P63104 (AlphaFold model)
Glucocorticoid receptor	C, D	protein	13	Homo sapiens	P04150 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>8A9G_1 14-3-3 protein zeta/delta (chains A, B)
GAMGSMDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEERNLLSVAYKNVVGAR
RSSWRVVSSIEQKTEGAEKKQQMAREYREKIETELRDICNDVLSLLEKFLIPNASQAESK
VFYLKMKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISKKEMQPTHPIRLGLALNFS
VFYYEILNSPEKACSLAKTAFDEAIAELDTLSEESYKDSTLIMQLLRDNLTLWTS

Sequence of entity 2 (C, D), FASTA

>8A9G_2 Glucocorticoid receptor (chains C, D)
KTIVPATLPQLTP

Ligands and cofactors

ID	Name	Formula	Copies
QJK	5-[(2~{R})-3-(4-chlorophenyl)carbonyl-2-(4-nitrophenyl)-4-oxidanyl-5-oxidanylid…	C24 H15 Cl N2 O8	2
MG	Magnesium ion	Mg	1
BTB	2-[bis-(2-hydroxy-ethyl)-amino]-2-hydroxymethyl-propane-1,3-diol	C8 H19 N O5	2

Primary citation

Designing Selective Drug-like Molecular Glues for the Glucocorticoid Receptor/14-3-3 Protein-Protein Interaction. Pallesen, J.S., Munier, C.C., Bosica, F. et al. J Med Chem (2022) 65:16818-16828. DOI 10.1021/acs.jmedchem.2c01635 · 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…
1QJA 2.0 Å, 14-3-3 zeta/phosphopeptide complex (mode 2)
1QJB 2.0 Å, 14-3-3 zeta/phosphopeptide complex (mode 1)

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