› 1px2

X-ray diffraction
2.23Å resolution

Crystal Structure of Rat Synapsin I C Domain Complexed to Ca.ATP (Form 1)

Released:
DOI: 10.2210/pdb1px2/pdb
PDB entry 1px2 coloured by chain, front view.
PDB entry 1px2 coloured by chain, side view.
PDB entry 1px2 coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Tetramerization and ATP binding by a protein comprising the A, B, and C domains of rat synapsin I.
Brautigam CA, Chelliah Y, Deisenhofer J
J Biol Chem 279 11948-56 (2004)
PMID: 14688264

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140834 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Synapsin-1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 422 amino acids
Theoretical weight: 45.54 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P09951 (Residues: 2-421; Coverage: 60%)
Gene name: Syn1
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand CA 2 x CA
Ligand ATP 2 x ATP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: P6522
Unit cell:
a: 96Å b: 96Å c: 305.8Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.205 0.203 0.24
Expression system: Escherichia coli BL21(DE3)

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Citations

2 review citations

Synapsin Isoforms and Synaptic Vesicle Trafficking.
Song et al. (2015)
1 more

1 mention without citation

Binding of protein kinase inhibitors to synapsin I inferred from pair-wise binding site similarity measurements.
Defranchi et al. (2010)