PDBe 3sv1

X-ray diffraction
3.3Å resolution

Crystal structure of APP peptide bound rat Mint2 PARM

Released:
Source organisms:
Primary publication:
Open-closed motion of Mint2 regulates APP metabolism.
J Mol Cell Biol (2012)
PMID: 22730553

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
C31 Chains: D, E, F
Molecule details ›
Chains: D, E, F
Length: 14 amino acids
Theoretical weight: 1.77 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P05067 (Residues: 754-767; Coverage: 2%)
Gene names: A4, AD1, APP
Amyloid-beta A4 precursor protein-binding family A member 2 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 190 amino acids
Theoretical weight: 21.29 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: O35431 (Residues: 365-552; Coverage: 25%)
Gene names: Apba2, Mint2
Sequence domains: Phosphotyrosine interaction domain (PTB/PID)
Structure domains: Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: C2
Unit cell:
a: 151.119Å b: 52.092Å c: 121.282Å
α: 90° β: 127.8° γ: 90°
R-values:
R R work R free
0.243 0.243 0.301
Expression systems:
  • Not provided
  • Escherichia coli