Structure analysis

Crystal structure of human 14-3-3 zeta in complex with CFTR R-domain peptide pS753-pS768

X-ray diffraction
2.1Å resolution
Source organism: Homo sapiens
Assembly composition:
hetero trimer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero trimer
Accessible surface area: 22400 Å2
Buried surface area: 5800 Å2
Dissociation area: 1,700 Å2
Dissociation energy (ΔGdiss): 18 kcal/mol
Dissociation entropy (TΔSdiss): 13 kcal/mol
Interface energy (ΔGint): -58 kcal/mol
Symmetry number: 1

Macromolecules

Chains: A, B
Length: 230 amino acids
Theoretical weight: 26.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P63104 (Residues: 1-230; Coverage: 94%)
Gene name: YWHAZ
Pfam: 14-3-3 protein
InterPro:
CATH: 14-3-3 domain

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Chain: C
Length: 28 amino acids
Theoretical weight: 3.26 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P13569 (Residues: 747-774; Coverage: 2%)
Gene names: ABCC7, CFTR
InterPro: CFTR regulator domain

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