8EQH: 14-3-3 protein beta/alpha

The crystal structure of 14-3-3 Beta containing 3-nitrotyrosine at position Y213. Determined by X-ray diffraction at 1.9 Å resolution. Released 25 Jan 2023.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,782
Mol. weight: 56.56 kDa
Released: 25 Jan 2023

Explore 8EQH in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8EQH contains 26 α-helices and 0 β-strands across 2 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	36-39	4
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	138-161	24
α-helix	167-178	12
α-helix	179-183	5
α-helix	187-202	16
α-helix	210-231	22

Chain B: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	5-17	13
α-helix	21-33	13
α-helix	37-39	3
α-helix	40-69	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	187-204	18
α-helix	210-230	21

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
14-3-3 protein beta/alpha	A, B	protein	245	Homo sapiens	P31946 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>8EQH_1 14-3-3 protein beta/alpha (chains A, B)
MTMDKSELVQKAKLAEQAERYDDMAAAMKAVTEQGHELSNEERNLLSVAYKNVVGARRSS
WRVISSIEQKTERNEKKQQMGKEYREKIEAELQDICNDVLELLDKYLIPNATQPESKVFY
LKMKGDYFRYLSEVASGDNKQTTVSNSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFY
YEILNSPEKACSLAKTAFDEAIAELDTLNEESYKDSTLIMQLLRDNLTLWTSENQGDEGE
NLYFQ

Primary citation

Genetic encoding of 3-nitro-tyrosine reveals the impacts of 14-3-3 nitration on client binding and dephosphorylation. Zhu, P., Nguyen, K.T., Estelle, A.B. et al. Protein Sci (2023) 32:e4574-e4574. DOI 10.1002/pro.4574 · 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
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

Browse structure collections

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