›3sv1

X-ray diffraction
3.3Å resolution

Crystal structure of APP peptide bound rat Mint2 PARM

Released:
PDB entry 3sv1 coloured by chain, front view.
PDB entry 3sv1 coloured by chain, side view.
PDB entry 3sv1 coloured by chain, top view.
Primary publication:
Open-closed motion of Mint2 regulates APP metabolism.
J Mol Cell Biol5 48-56 (2013)
PMID: 22730553

Function and BiologyDetails

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysisDetails

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-128682 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Amyloid-beta A4 precursor protein-binding family A member 2Chains: 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)
C31Chains: 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

Ligands and Environments

No bound ligands
No modified residues

Experiments and ValidationDetails

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:
RR workR free
0.243 0.243 0.301
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

1 review citation

5 mentions without citation

PDB-REDO

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