5my9

X-ray diffraction
1.33Å resolution

Crystal structure of human 14-3-3 sigma in complex with LRRK2 peptide pS935

Released:
Source organism: Homo sapiens
Primary publication:
Structural interface between LRRK2 and 14-3-3 protein.
Biochem J 474 1273-1287 (2017)
PMID: 28202711

Function and Biology Details

Reaction catalysed:
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-152161 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
14-3-3 protein sigma Chain: A
Molecule details ›
Chain: A
Length: 236 amino acids
Theoretical weight: 26.54 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P31947 (Residues: 1-231; Coverage: 93%)
Gene names: HME1, SFN
Sequence domains: 14-3-3 protein
Structure domains: 14-3-3 domain
Leucine-rich repeat serine/threonine-protein kinase 2 Chain: P
Molecule details ›
Chain: P
Length: 13 amino acids
Theoretical weight: 1.57 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q5S007 (Residues: 929-941; Coverage: 1%)
Gene names: LRRK2, PARK8

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: C2221
Unit cell:
a: 82.291Å b: 112.03Å c: 62.43Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.186 0.2
Expression systems:
  • Escherichia coli
  • Not provided