7nmz

X-ray diffraction
2.3Å resolution

Structure of 14-3-3 eta in complex with Nedd4-2(335-455) containing two 14-3-3 binding motifs Ser342 and Ser448

Released:

Function and Biology Details

Reactions catalysed:
(1a) S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [HECT-type E3 ubiquitin transferase]-L-cysteine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + S-ubiquitinyl-[HECT-type E3 ubiquitin transferase]-L-cysteine
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-cysteine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-S-ubiquitinyl-L-cysteine

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-170091 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
14-3-3 protein eta Chains: AA, BA
Molecule details ›
Chains: AA, BA
Length: 236 amino acids
Theoretical weight: 27.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q04917 (Residues: 1-234; Coverage: 95%)
Gene names: YWHA1, YWHAH
Sequence domains: 14-3-3 protein
E3 ubiquitin-protein ligase NEDD4-like Chain: C
Molecule details ›
Chain: C
Length: 125 amino acids
Theoretical weight: 13.44 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q96PU5 (Residues: 335-455; Coverage: 12%)
Gene names: KIAA0439, NEDD4L, NEDL3
Sequence domains: WW domain

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: Excillum MetalJet D2+ 70 kV
Spacegroup: C2
Unit cell:
a: 117.86Å b: 58.95Å c: 106.76Å
α: 90° β: 90.693° γ: 90°
R-values:
R R work R free
0.201 0.199 0.235
Expression system: Escherichia coli BL21(DE3)