6A5Q: 14-3-3 beta

Structure of 14-3-3 beta in complex with TFEB 14-3-3 binding motif. Determined by X-ray diffraction at 2.0 Å resolution. Released 13 Feb 2019.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Homo sapiens
Chains: 6
Atoms: 6,276
Mol. weight: 90.22 kDa
Ligands: MLA
Released: 13 Feb 2019

Explore 6A5Q in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6A5Q contains 41 α-helices and 0 β-strands across 3 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	5-17	13
α-helix	21-33	13
α-helix	40-70	31
α-helix	75-102	28
α-helix	103-107	5
α-helix	108-110	3
α-helix	114-134	21
α-helix	137-161	25
α-helix	167-178	12
α-helix	179-183	5
α-helix	187-203	17
α-helix	205-207	3
α-helix	213-232	20

Chain B: 14 helices, 0 β-strands

Element	Residues	Length
α-helix	5-17	13
α-helix	21-33	13
α-helix	36-39	4
α-helix	40-69	30
α-helix	75-102	28
α-helix	103-107	5
α-helix	108-110	3
α-helix	114-134	21
α-helix	137-161	25
α-helix	167-178	12
α-helix	179-183	5
α-helix	187-203	17
α-helix	205-207	3
α-helix	210-231	22

Chain C: 14 helices, 0 β-strands

Element	Residues	Length
α-helix	5-17	13
α-helix	21-33	13
α-helix	37-39	3
α-helix	40-68	29
α-helix	79-102	24
α-helix	103-107	5
α-helix	108-110	3
α-helix	114-134	21
α-helix	137-161	25
α-helix	167-178	12
α-helix	179-183	5
α-helix	187-203	17
α-helix	205-207	3
α-helix	210-232	23

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
14-3-3 protein beta/alpha	A, B, C	protein	250	Homo sapiens	P31946 (AlphaFold model)
TFEB pS211-peptide	D, E, F	protein	15	Homo sapiens

Sequence of entity 1 (A, B, C), FASTA

>6A5Q_1 14-3-3 protein beta/alpha (chains A, B, C)
GPGSMTMDKSELVQKAKLAEQAERYDDMAAAMKAVTEQGHELSNEERNLLSVAYKNVVGA
RRSSWRVISSIEQKTERNEKKQQMGKEYREKIEAELQDICNDVLELLDKYLIPNATQPES
KVFYLKMKGDYFRYLSEVASGDNKQTTVSNSQQAYQEAFEISKKEMQPTHPIRLGLALNF
SVFYYEILNSPEKACSLAKTAFDEAIAELDTLNEESYKDSTLIMQLLRDNLTLWTSENQG
DEGDAGEGEN

Sequence of entity 2 (D, E, F), FASTA

>6A5Q_2 TFEB  pS211-peptide (chains D, E, F)
LVGVTSSSCPADLTQ

Ligands and cofactors

ID	Name	Formula	Copies
MLA	Malonic acid	C3 H4 O4	3

Primary citation

YWHA/14-3-3 proteins recognize phosphorylated TFEB by a noncanonical mode for controlling TFEB cytoplasmic localization. Xu, Y., Ren, J., He, X. et al. Autophagy (2019) 15:1017-1030. DOI 10.1080/15548627.2019.1569928 · PubMed

Other PDB entries of the same protein (UniProt P31946 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8EQ8 1.5 Å, The crystal structure of 14-3-3 Beta containing 3-nitrotyrosine at position Y130
5N10 1.6 Å, Cucurbit[8]uril and 14-3-3 based binary bivalent supramolecular-protein assembly platform
6HEP 1.86 Å, Crystal structure of human 14-3-3 beta in complex with CFTR R-domain peptide pS753-pS768
8EQH 1.9 Å, The crystal structure of 14-3-3 Beta containing 3-nitrotyrosine at position Y213
6YGJ 2.07 Å, small-molecule stabilizer of 14-3-3 and the Carbohydrate Response Element Binding…
4DNK 2.2 Å, Crystal structure of a tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation…
6GN8 2.34 Å, Exoenzyme S from Pseudomonas aeruginosa in complex with human 14-3-3 protein beta,…
2BQ0 2.5 Å, 14-3-3 Protein Beta (Human)
6GNK 2.55 Å, Exoenzyme S from Pseudomonas aeruginosa in complex with human 14-3-3 protein beta,…
9GCP 2.59 Å, ChREBP/14-3-3 complex stabilized by AMP
2C23 2.65 Å, 14-3-3 Protein Beta (Human) in complex with exoenzyme S peptide
6BYK 3.0 Å, Structure of 14-3-3 beta/alpha bound to O-ClcNAc peptide

Browse structure collections

About this viewer

MolViewer shows 6A5Q directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.