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Crystal structure of the full-length wild-type PKA ria holoenzyme

Analyse Crystal structure of the full-length wild-type PKA ria holoenzyme in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6NO7
Type
protein
Length
2,491 residues
Chains
8
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt
P17612, P00514
Ligands
ATP, MG

Structure

x-ray diffraction · 7 distinct chains.

ChainMoleculeTypeResiduesSecondary structureUniProt
A—protein336—P17612
B—protein285—P00514
C—protein340—P17612
D—protein286—P00514
E—protein339—P17612
F, H—protein284—P00514
G—protein337—P17612

Ligands and binding sites

  • ATP · Adenosine-5'-triphosphate · ligand · 2 copies · chains E, F, G
  • MG · Magnesium ion · metal · 4 copies · chains E, G

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

Compared structures

  • 6NO7 · Crystal Structure of the full-length wild-type PKA RIa Holoenzyme · the same entry in another collection · chain H against H, TM-score 1.00
  • P17612 · AlphaFold monomer V2.0 prediction for camp-dependent protein kinase catalytic subunit… · a predicted model of the same protein · chain A against A, TM-score 0.99
  • P00514 · AlphaFold monomer V2.0 prediction for camp-dependent protein kinase type I-alpha… · a predicted model of the same protein · chain D against A, TM-score 0.97

Analyse

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