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Crystal structure of PKA ri alpha DIMERIZATION/DOCKING domain

Analyse Crystal structure of PKA ri alpha DIMERIZATION/DOCKING domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3IM3
Type
protein
Length
50 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Camp-dependent protein kinase type I-alpha regulatory subunit
UniProt
P00514

Structure

x-ray diffraction · 1 distinct chain · 84% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACamp-dependent protein kinase type I-alpha regulatory subunitprotein5084% helix, 0% strandP00514

Ligands and binding sites

  • FMT · Formic acid · additive · 2 copies · chains A

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

Compared structures

  • 3IM3 · Crystal structure of PKA RI alpha dimerization/docking domain · the same entry in another collection · chain A against A, TM-score 1.00
  • P00514 · AlphaFold monomer V2.0 prediction for camp-dependent protein kinase type I-alpha… · a predicted model of the same protein · chain A against A, TM-score 0.82

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