6BYK: 14-3-3 beta/alpha

Structure of 14-3-3 beta/alpha bound to O-ClcNAc peptide. Determined by X-ray diffraction at 3.0 Å resolution. Released 9 May 2018.

Method: X-ray diffraction
Resolution: 3.0 Å
Organisms: Homo sapiens, synthetic construct
Chains: 8
Atoms: 7,565
Mol. weight: 111.39 kDa
Ligands: NAG
Released: 9 May 2018

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

Secondary structure: helices and β-sheets

6BYK contains 49 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	5-17	13
α-helix	21-32	12
α-helix	37-39	3
α-helix	40-67	28
α-helix	75-102	28
α-helix	103-107	5
α-helix	108-110	3
α-helix	114-133	20
α-helix	138-161	24
α-helix	167-182	16
α-helix	187-202	16
α-helix	210-213	4
α-helix	214-231	18

Chain B: 12 helices, 0 β-strands

Element	Residues	Length
α-helix	5-17	13
α-helix	21-32	12
α-helix	37-39	3
α-helix	40-69	30
α-helix	75-102	28
α-helix	103-107	5
α-helix	114-132	19
α-helix	138-161	24
α-helix	167-182	16
α-helix	187-204	18
α-helix	205-207	3
α-helix	213-230	18

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	40-70	31
α-helix	75-102	28
α-helix	103-107	5
α-helix	108-110	3
α-helix	114-133	20
α-helix	138-161	24
α-helix	167-178	12
α-helix	179-183	5
α-helix	187-202	16
α-helix	210-231	22

Chain D: 11 helices, 0 β-strands

Element	Residues	Length
α-helix	5-18	14
α-helix	21-33	13
α-helix	37-39	3
α-helix	40-68	29
α-helix	75-102	28
α-helix	103-107	5
α-helix	114-133	20
α-helix	138-161	24
α-helix	167-182	16
α-helix	187-202	16
α-helix	213-230	18

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
14-3-3 protein beta/alpha	A, B, C, D	protein	230	Homo sapiens	P31946 (AlphaFold model)
ATPPVSQASSTT O-GlcNac peptide	G, J, K, R	protein	12	synthetic construct

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

>6BYK_1 14-3-3 protein beta/alpha (chains A, B, C, D)
MDKSELVQKAKLAEQAERYDDMAAAMKAVTEQGHELSNEERNLLSVAYKNVVGARRSSWR
VISSIEQKTERNEKKQQMGKEYREKIEAELQDICNDVLELLDKYLIPNATQPESKVFYLK
MKGDYFRYLSEVASGDNKQTTVSNSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYE
ILNSPEKACSLAKTAFDEAIAELDTLNEESYKDSTLIMQLLRDNLTLWTS

Sequence of entity 2 (G, J, K, R), FASTA

>6BYK_2 ATPPVSQASSTT O-GlcNac peptide (chains G, J, K, R)
ATPPVSQASSTT

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	4

Primary citation

Structural basis of O-GlcNAc recognition by mammalian 14-3-3 proteins. Toleman, C.A., Schumacher, M.A., Yu, S.H. et al. Proc Natl Acad Sci U S A (2018) 115:5956-5961. DOI 10.1073/pnas.1722437115 · 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
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

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