2C74: 14-3-3 Protein Eta (Human) Complexed to Peptide

14-3-3 Protein Eta (Human) Complexed to Peptide. Determined by X-ray diffraction at 2.7 Å resolution. Released 2 Dec 2005.

Method
X-ray diffraction
Resolution
2.7 Å
Organisms
HOMO SAPIENS, synthetic construct
Chains
4
Atoms
3,672
Mol. weight
58.78 kDa
Ligands
CIT
Released
2 Dec 2005

Explore 2C74 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2C74 contains 28 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.

Chains A and B: 14 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix3-1614
α-helix20-3112
α-helix36-383
α-helix39-7234
α-helix76-10328
α-helix104-1085
α-helix117-13519
α-helix140-16425
α-helix170-18112
α-helix182-1865
α-helix190-20617
α-helix208-2103
α-helix213-2153
α-helix216-23419

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
14-3-3 protein etaA, Bprotein247HOMO SAPIENSQ04917 (AlphaFold model)
Consensus peptide mode 1 for 14-3-3 proteinsP, Qprotein7synthetic construct
Sequence of entity 1 (A, B), FASTA
>2C74_1 14-3-3 PROTEIN ETA (chains A, B)
SMGDREQLLQRARLAEQAERYDDMASAMKAVTELNEPLSNEDRNLLSVAYKNVVGARRSS
WRVISSIEQKTMADGNEKKLEKVKAYREKIEKELETVCNDVLSLLDKFLIKNCNDFQYES
KVFYLKMKGDYYRYLAEVASGEKKNSVVEASEAAYKEAFEISKEQMQPTHPIRLGLALNF
SVFYYEIQNAPEQACLLAKQAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQQD
EEAGEGN
Sequence of entity 2 (P, Q), FASTA
>2C74_2 CONSENSUS PEPTIDE MODE 1 FOR 14-3-3 PROTEINS (chains P, Q)
RRQRSAP

Ligands and cofactors

IDNameFormulaCopies
CITCitric acidC6 H8 O71

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) 103:17237-17242. 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:

Browse structure collections

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