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Two structures of the catalytic domain of phosphorylase, kinase: an active protein kinase complexed with nucleotide, substrate-analogue and product

Analyse Two structures of the catalytic domain of phosphorylase, kinase: an active… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1PHK
Type
protein
Length
277 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Phosphorylase kinase
EC
2.7.1.38
UniProt
P00518
Ligands
ATP, MN
Pockets
1 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APhosphorylase kinase (EC 2.7.1.38)protein27740% helix, 19% strandP00518

Ligands and binding sites

  • ATP · Adenosine-5'-triphosphate · ligand · chains A
  • MN · Manganese (II) ion · metal · 2 copies · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14050.680.8044MN, ATP

Compared structures

  • 1PHK · Two structures of the catalytic domain of phosphorylase, kinase: an active protein kinase… · the same entry in another collection · chain A against A, TM-score 1.00
  • P00518 · AlphaFold monomer V2.0 prediction for phosphorylase B kinase gamma catalytic chain… · a predicted model of the same protein · chain A against A, TM-score 0.98

Analyse

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