PDBe 1ib1

X-ray diffraction
2.7Å resolution

CRYSTAL STRUCTURE OF THE 14-3-3 ZETA:SEROTONIN N-ACETYLTRANSFERASE COMPLEX

Released:

Function and Biology Details

Reaction catalysed:
Acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
14-3-3 protein zeta/delta Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 245 amino acids
Theoretical weight: 27.78 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: NEW P63104 (Residues: 1-245; Coverage: 100%)
Gene name: YWHAZ
Sequence domains: 14-3-3 protein
Structure domains: 14-3-3 domain
Serotonin N-acetyltransferase Chains: E, F, G, H
Molecule details ›
Chains: E, F, G, H
Length: 200 amino acids
Theoretical weight: 22.27 KDa
Source organism: Ovis aries
Expression system: Escherichia coli
UniProt:
  • Canonical: NEW Q29495 (Residues: 2-201; Coverage: 97%)
Gene names: AANAT, SNAT
Sequence domains: Acetyltransferase (GNAT) family
Structure domains: Aminopeptidase

Ligands and Environments


Cofactor: Ligand COT 4 x COT
No bound ligands

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P1
Unit cell:
a: 74.717Å b: 75.078Å c: 101.78Å
α: 90.144° β: 90.063° γ: 63.044°
R-values:
R R work R free
0.21 0.204 0.228
Expression systems:
  • Escherichia coli BL21(DE3)
  • Escherichia coli