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Structure of CDK2/cyclin A M246Q, S247EN

Analyse Structure of CDK2/cyclin A M246Q, S247EN in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6SG4
Type
protein
Length
1,038 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.43
Source
Homo sapiens
Molecule
Cyclin-dependent kinase 2; Cyclin-A2
EC
2.7.11.22
UniProt
P24941, P20248
Pockets
13 · best druggability 0.80

Structure

x-ray diffraction · resolution 2.43 · 4 distinct chains · 50% helix, 6% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACyclin-dependent kinase 2 (EC 2.7.11.22)protein26238% helix, 12% strandP24941
BCyclin-A2protein25864% helix, 0% strandP20248
CCyclin-dependent kinase 2 (EC 2.7.11.22)protein26136% helix, 11% strandP24941
DCyclin-A2protein25762% helix, 0% strandP20248

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11520.800.9725empty
21510.780.9523empty
32780.630.8143empty
43090.590.7840empty
52230.550.7832empty

Interfaces

3 interfaces between chains.

  • A–B · 1680 Ų buried · 25 hydrogen bonds · protein-protein
  • C–D · 1594 Ų buried · 18 hydrogen bonds · protein-protein
  • A–C · 636 Ų buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (phosphorylation).

Compared structures

  • 6SG4 · Structure of CDK2/CYCLIN a M246Q, S247EN · the same entry in another collection · chain D against D, TM-score 1.00
  • P20248 · AlphaFold monomer V2.0 prediction for cyclin-A2 (P20248) · a predicted model of the same protein · chain D against A, TM-score 0.99
  • P24941 · AlphaFold monomer V2.0 prediction for cyclin-dependent kinase 2 (P24941) · a predicted model of the same protein · chain A against A, TM-score 0.91

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