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RIP2 Kinase Catalytic Domain (1 - 310)

Analyse RIP2 Kinase Catalytic Domain (1 - 310) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5AR2
Type
protein
Length
562 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.44
Source
HOMO SAPIENS
Molecule
Receptor-interacting SERINE/THREONINE-protein kinase 2
EC
2.7.11.1
UniProt
O43353
Ligands
CA
Pockets
7 · best druggability 0.83

Structure

x-ray diffraction · resolution 2.44 · 2 distinct chains · 38% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AReceptor-interacting SERINE/THREONINE-protein kinase 2 (EC 2.7.11.1)protein27739% helix, 16% strandO43353
BReceptor-interacting SERINE/THREONINE-protein kinase 2 (EC 2.7.11.1)protein28538% helix, 17% strandO43353

Ligands and binding sites

  • CA · Calcium ion · metal · chains B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110750.830.8485empty
23980.640.7844empty
32820.590.7828empty
41340.480.7826empty
5650.370.7917empty

Interfaces

1 interface between chains.

  • A–B · 1881 Ų buried · 21 hydrogen bonds · protein-protein

Compared structures

  • 5AR2 · RIP2 kinase catalytic domain (1 - 310) · the same entry in another collection · chain A against A, TM-score 1.00
  • O43353 · AlphaFold monomer V2.0 prediction for receptor-interacting SERINE/THREONINE-protein… · a predicted model of the same protein · chain A against A, TM-score 0.97

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