2C63: 14-3-3 Protein Eta (Human) Complexed to Peptide

14-3-3 Protein Eta (Human) Complexed to Peptide. Determined by X-ray diffraction at 2.15 Å resolution. Released 21 Nov 2005.

Method: X-ray diffraction
Resolution: 2.15 Å
Organism: HOMO SAPIENS
Chains: 8
Atoms: 7,886
Mol. weight: 116.3 kDa
Released: 21 Nov 2005

Explore 2C63 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2C63 contains 50 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: 12 helices, 0 β-strands

Element	Residues	Length
α-helix	4-16	13
α-helix	20-31	12
α-helix	39-73	35
α-helix	76-103	28
α-helix	104-108	5
α-helix	117-137	21
α-helix	140-164	25
α-helix	170-181	12
α-helix	182-186	5
α-helix	190-206	17
α-helix	208-210	3
α-helix	216-234	19

Chain B: 12 helices, 0 β-strands

Element	Residues	Length
α-helix	4-17	14
α-helix	20-31	12
α-helix	39-73	35
α-helix	76-103	28
α-helix	104-108	5
α-helix	117-135	19
α-helix	140-164	25
α-helix	170-181	12
α-helix	182-186	5
α-helix	190-206	17
α-helix	208-210	3
α-helix	216-234	19

Chain C: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	4-16	13
α-helix	20-32	13
α-helix	36-38	3
α-helix	39-73	35
α-helix	76-103	28
α-helix	104-108	5
α-helix	117-135	19
α-helix	140-164	25
α-helix	170-181	12
α-helix	182-187	6
α-helix	190-206	17
α-helix	208-210	3
α-helix	216-234	19

Chain D: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	4-16	13
α-helix	20-31	12
α-helix	36-38	3
α-helix	39-73	35
α-helix	76-103	28
α-helix	104-108	5
α-helix	117-135	19
α-helix	140-164	25
α-helix	170-181	12
α-helix	182-187	6
α-helix	190-206	17
α-helix	208-210	3
α-helix	216-234	19

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
14-3-3 protein eta	A, B, C, D	protein	247	HOMO SAPIENS	Q04917 (AlphaFold model)
Consensus peptide for 14-3-3 proteins	P, Q, R, S	protein	6	HOMO SAPIENS

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

>2C63_1 14-3-3 PROTEIN ETA (chains A, B, C, D)
SMGDREQLLQRARLAEQAERYDDMASAMKAVTELNEPLSNEDRNLLSVAYKNVVGARRSS
WRVISSIEQKTMADGNEKKLEKVKAYREKIEKELETVCNDVLSLLDKFLIKNCNDFQYES
KVFYLKMKGDYYRYLAEVASGEKKNSVVEASEAAYKEAFEISKEQMQPTHPIRLGLALNF
SVFYYEIQNAPEQACLLAKQAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQQD
EEAGEGN

Sequence of entity 2 (P, Q, R, S), FASTA

>2C63_2 CONSENSUS PEPTIDE FOR 14-3-3 PROTEINS (chains P, Q, R, S)
RAISLP

Primary citation

Structural Basis for Protein-Protein Interactions in the 14-3-3 Protein Family. Yang, X., Lee, W.H., Sobott, F. et al. Proc Natl Acad Sci U S A (2006) 103:17237. DOI 10.1073/PNAS.0605779103 · PubMed

Other PDB entries of the same protein (UniProt Q04917 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7NMZ 2.3 Å, Structure of 14-3-3 eta in complex with Nedd4-2(335-455) containing two 14-3-3 binding…
2C74 2.7 Å, 14-3-3 Protein Eta (Human) Complexed to Peptide
9R2I 3.3 Å, Cryo-EM structure of the complex CDK16:CCNY:14-3-3
9R2N 3.83 Å, Cryo-EM structure of the complex CCNY:14-3-3

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