6QZR: 14-3-3 sigma

14-3-3 sigma in complex with FOXO1 pT24 peptide. Determined by X-ray diffraction at 2.3 Å resolution. Released 31 Jul 2019.

Method: X-ray diffraction
Resolution: 2.3 Å
Organism: Homo sapiens
Chains: 16
Atoms: 15,184
Mol. weight: 239.2 kDa
Ligands: B3P
Released: 31 Jul 2019

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

Secondary structure: helices and β-sheets

6QZR contains 99 α-helices and 0 β-strands across 9 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	3-15	13
α-helix	19-30	12
α-helix	35-37	3
α-helix	38-67	30
α-helix	80-102	23
α-helix	103-107	5
α-helix	114-132	19
α-helix	137-161	25
α-helix	167-182	16
α-helix	187-202	16
α-helix	215-230	16

Chain B: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	3-15	13
α-helix	19-30	12
α-helix	34-36	3
α-helix	38-67	30
α-helix	80-102	23
α-helix	103-107	5
α-helix	114-134	21
α-helix	137-161	25
α-helix	167-178	12
α-helix	179-183	5
α-helix	187-202	16
α-helix	205-207	3
α-helix	213-230	18

Chain C: 12 helices, 0 β-strands

Element	Residues	Length
α-helix	3-15	13
α-helix	19-30	12
α-helix	34-37	4
α-helix	38-67	30
α-helix	80-102	23
α-helix	103-107	5
α-helix	114-132	19
α-helix	137-161	25
α-helix	167-178	12
α-helix	179-183	5
α-helix	187-202	16
α-helix	210-230	21

Chain D: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	3-15	13
α-helix	19-30	12
α-helix	34-37	4
α-helix	38-65	28
α-helix	80-102	23
α-helix	103-107	5
α-helix	114-134	21
α-helix	140-160	21
α-helix	167-178	12
α-helix	179-183	5
α-helix	184	1
α-helix	187-204	18
α-helix	217-228	12

Chain E: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	3-15	13
α-helix	19-30	12
α-helix	34-36	3
α-helix	38-68	31
α-helix	80-102	23
α-helix	103-107	5
α-helix	114-132	19
α-helix	137-161	25
α-helix	167-178	12
α-helix	179-183	5
α-helix	187-202	16
α-helix	205-207	3
α-helix	212-229	18

Chain F: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	3-15	13
α-helix	19-30	12
α-helix	35-36	2
α-helix	38-68	31
α-helix	80-102	23
α-helix	103-107	5
α-helix	114-134	21
α-helix	137-161	25
α-helix	167-178	12
α-helix	179-183	5
α-helix	187-202	16
α-helix	210-212	3
α-helix	213-229	17

Chain G: 11 helices, 0 β-strands

Element	Residues	Length
α-helix	3-15	13
α-helix	19-30	12
α-helix	34-37	4
α-helix	38-68	31
α-helix	80-102	23
α-helix	103-107	5
α-helix	114-132	19
α-helix	138-160	23
α-helix	167-182	16
α-helix	187-202	16
α-helix	214-230	17

Chain H: 12 helices, 0 β-strands

Element	Residues	Length
α-helix	3-15	13
α-helix	19-30	12
α-helix	34-37	4
α-helix	38-68	31
α-helix	80-102	23
α-helix	103-107	5
α-helix	114-132	19
α-helix	138-161	24
α-helix	167-182	16
α-helix	187-203	17
α-helix	205-207	3
α-helix	212-229	18

1 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
14-3-3 protein sigma	A, B, C, D, E, F, G, H	protein	253	Homo sapiens	P31947 (AlphaFold model)
Forkhead box protein O1	J, M, N, O, P, R, T, U	protein	11	Homo sapiens	Q12778 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F, G, H), FASTA

>6QZR_1 14-3-3 protein sigma (chains A, B, C, D, E, F, G, H)
GAMGSMERASLIQKAKLAEQAERYEDMAAFMKGAVEKGEELSCEERNLLSVAYKNVVGGQ
RAAWRVLSSIEQKSNEEGSEEKGPEVREYREKVETELQGVCDTVLGLLDSHLIKEAGDAE
SRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAMDISKKEMPPTNPIRLGLALN
FSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWTADNA
GEEGGEAPQEPQS

Sequence of entity 2 (J, M, N, O, P, R, T, U), FASTA

>6QZR_2 Forkhead box protein O1 (chains J, M, N, O, P, R, T, U)
RPRSCTWPLPR

Ligands and cofactors

ID	Name	Formula	Copies
B3P	2-[3-(2-hydroxy-1,1-dihydroxymethyl-ethylamino)-propylamino]-2-hydroxymethyl-pr…	C11 H26 N2 O6	4

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

Primary citation

AMPK and AKT protein kinases hierarchically phosphorylate the N-terminus of the FOXO1 transcription factor, modulating interactions with 14-3-3 proteins. Saline, M., Badertscher, L., Wolter, M. et al. J Biol Chem (2019) 294:13106-13116. DOI 10.1074/jbc.RA119.008649 · PubMed

Other PDB entries of the same protein (UniProt P31947 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3IQU 1.05 Å, Crystal Structure of human 14-3-3 sigma in Complex with Raf1 peptide (6mer)
7AZ2 1.08 Å, 14-3-3 sigma with Pin1 binding site pS72 and covalently bound LvD1014
6HMT 1.1 Å, Ternary complex of Estrogen Receptor alpha peptide and 14-3-3 sigma C42 mutant bound to…
7BAA 1.1 Å, Cys-42-tethered stabilizer 12 of 14-3-3(sigma)/ERa PPI
8BZC 1.1 Å, co-soaked stabilizers for ERa - 14-3-3 interaction (884_AZ244)
8BZW 1.1 Å, Co-soaked stabilizers for ERa - 14-3-3 interaction (844_AZ210)
8C04 1.1 Å, Co-soaked stabilizers for ERa - 14-3-3 interaction (884_AZ354)
9GG8 1.1 Å, Crystal structure of 14-3-3 sigma dC - C38N in complex with Tau pS214 peptide and…
8ANC 1.11 Å, 14-3-3 sigma sirtuin-3 phospho-peptide complex
6Y1J 1.13 Å, 14-3-3 sigma in complex with IkappaBalpha pS63 peptide
6G6X 1.13 Å, 14-3-3sigma in complex with a P129beta3P mutated YAP pS127 phosphopeptide
6NV2 1.13 Å, 14-3-3 sigma with RelA/p65 binding site pS45 in complex with DP005

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