3LW1: 14-3-3 protein sigma

Binary complex of 14-3-3 sigma and p53 pT387-peptide. Determined by X-ray diffraction at 1.28 Å resolution. Released 23 Mar 2010.

Method: X-ray diffraction
Resolution: 1.28 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,559
Mol. weight: 29.5 kDa
Ligands: MG
Released: 23 Mar 2010

Explore 3LW1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3LW1 contains 15 α-helices and 0 β-strands across 1 chain. 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: 15 helices, 0 β-strands

Element	Residues	Length
α-helix	3-15	13
α-helix	19-31	13
α-helix	34-37	4
α-helix	38-69	32
α-helix	74-76	3
α-helix	80-102	23
α-helix	103-107	5
α-helix	108-110	3
α-helix	114-134	21
α-helix	140-161	22
α-helix	167-178	12
α-helix	179-183	5
α-helix	187-202	16
α-helix	205-207	3
α-helix	210-230	21

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
14-3-3 protein sigma	A	protein	253	Homo sapiens	P31947 (AlphaFold model)
peptide of Cellular tumor antigen p53	P	protein	9		P04637 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3LW1_1 14-3-3 protein sigma (chains A)
GAMGSMERASLIQKAKLAEQAERYEDMAAFMKGAVEKGEELSCEERNLLSVAYKNVVGGQ
RAAWRVLSSIEQKSNEEGSEEKGPEVREYREKVETELQGVCDTVLGLLDSHLIKEAGDAE
SRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAMDISKKEMPPTNPIRLGLALN
FSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWTADNA
GEEGGEAPQEPQS

Sequence of entity 2 (P), FASTA

>3LW1_2 peptide of Cellular tumor antigen p53 (chains P)
FKTEGPDSD

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	3

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

Primary citation

Structure of the p53 C-terminus bound to 14-3-3: Implications for stabilization of the p53 tetramer. Schumacher, B., Mondry, J., Thiel, P. et al. FEBS Lett (2010) 584:1443-1448. DOI 10.1016/j.febslet.2010.02.065 · 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

Browse structure collections

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