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Crystal structure of the C2A domain of rabphilin-3A

Analyse Crystal structure of the C2A domain of rabphilin-3A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2CHD
Type
protein
Length
128 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Rabphilin-3A
UniProt
P47709

Structure

x-ray diffraction · 1 distinct chain · 12% helix, 51% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARabphilin-3Aprotein12812% helix, 51% strandP47709

Ligands and binding sites

  • GOL · Glycerol · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

  • 2CHD · Crystal structure of the C2A domain of Rabphilin-3A · the same entry in another collection · chain A against A, TM-score 1.00
  • P47709 · AlphaFold monomer V2.0 prediction for rabphilin-3A (P47709) · a predicted model of the same protein · chain A against A, TM-score 0.94

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