6HEP: Human 14-3-3 beta

Crystal structure of human 14-3-3 beta in complex with CFTR R-domain peptide pS753-pS768. Determined by X-ray diffraction at 1.86 Å resolution. Released 24 Oct 2018.

Method: X-ray diffraction
Resolution: 1.86 Å
Organism: Homo sapiens
Chains: 6
Atoms: 8,373
Mol. weight: 114.88 kDa
Ligands: ETE
Released: 24 Oct 2018

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

Secondary structure: helices and β-sheets

6HEP contains 56 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: 14 helices, 0 β-strands

Element	Residues	Length
α-helix	5-17	13
α-helix	21-32	12
α-helix	37-39	3
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	187-205	19
α-helix	210-213	4
α-helix	214-231	18

Chain B: 15 helices, 0 β-strands

Element	Residues	Length
α-helix	0-2	3
α-helix	5-17	13
α-helix	21-33	13
α-helix	37-39	3
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	187-202	16
α-helix	205-207	3
α-helix	210-231	22

Chain C: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	5-17	13
α-helix	21-32	12
α-helix	37-38	2
α-helix	40-69	30
α-helix	75-102	28
α-helix	103-107	5
α-helix	114-132	19
α-helix	138-161	24
α-helix	167-178	12
α-helix	179-183	5
α-helix	187-205	19
α-helix	210-213	4
α-helix	214-229	16

Chain D: 14 helices, 0 β-strands

Element	Residues	Length
α-helix	0-2	3
α-helix	5-17	13
α-helix	21-33	13
α-helix	37-39	3
α-helix	40-70	31
α-helix	80-102	23
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	187-202	16
α-helix	215-230	16

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
14-3-3 protein beta/alpha	A, B, C, D	protein	235	Homo sapiens	P31946 (AlphaFold model)
Cystic fibrosis transmembrane conductance regulator	E, F	protein	28	Homo sapiens	P13569 (AlphaFold model)

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

>6HEP_1 14-3-3 protein beta/alpha (chains A, B, C, D)
MGSMTMDKSELVQKAKLAEQAERYDDMAAAMKAVTEQGHELSNEERNLLSVAYKNVVGAR
RSSWRVISSIEQKTERNEKKQQMGKEYREKIEAELQDICNDVLELLDKYLIPNATQPESK
VFYLKMKGDYFRYLSEVASGDNKQTTVSNSQQAYQEAFEISKKEMQPTHPIRLGLALNFS
VFYYEILNSPEKACSLAKTAFDEAIAELDTLNEESYKDSTLIMQLLRDNLTLWTS

Sequence of entity 2 (E, F), FASTA

>6HEP_2 Cystic fibrosis transmembrane conductance regulator (chains E, F)
AILPRISVISTGPTLQARRRQSVLNLMT

Ligands and cofactors

ID	Name	Formula	Copies
ETE	2-{2-[2-2-(methoxy-ethoxy)-ethoxy]-ethoxy}-ethanol	C9 H20 O5	2

Primary citation

A Thermodynamic Model for Multivalency in 14-3-3 Protein-Protein Interactions. Stevers, L.M., de Vink, P.J., Ottmann, C. et al. J Am Chem Soc (2018) 140:14498-14510. DOI 10.1021/jacs.8b09618 · 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
8EQH 1.9 Å, The crystal structure of 14-3-3 Beta containing 3-nitrotyrosine at position Y213
6A5Q 2.0 Å, Structure of 14-3-3 beta in complex with TFEB 14-3-3 binding motif
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

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