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Phosphorylated RSK4 N-terminal kinase domain in complex with AMP-pnp

Analyse Phosphorylated RSK4 N-terminal kinase domain in complex with AMP-pnp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6G76
Type
protein
Length
560 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ribosomal protein S6 kinase alpha-6
EC
2.7.11.1
UniProt
Q9UK32
Ligands
ANP, ZN
Pockets
6 · best druggability 0.65

Structure

x-ray diffraction · 2 distinct chains · 31% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARibosomal protein S6 kinase alpha-6 (EC 2.7.11.1)protein29133% helix, 22% strandQ9UK32
BRibosomal protein S6 kinase alpha-6 (EC 2.7.11.1)protein26928% helix, 23% strandQ9UK32

Ligands and binding sites

  • ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 3 copies · chains A, B
  • ZN · Zinc ion · metal · chains A

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

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12070.650.8433ANP
24960.650.7742empty
33060.630.8047ANP
42430.470.7337empty
51280.450.7721ANP

Interfaces

1 interface between chains.

  • A–B · 300 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

  • 6G76 · Phosphorylated RSK4 N-terminal Kinase Domain in complex with AMP-PNP · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9UK32 · AlphaFold monomer V2.0 prediction for ribosomal protein S6 kinase alpha-6 (Q9UK32) · a predicted model of the same protein · chain B against A, TM-score 0.86

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