MolNFT v1 · #90621 · protein
Thr 160 phosphorylated CDK2 wt - human cyclin A3 complex with ATP
4EOQ · Cyclin-dependent kinase 2: “Thr 160 phosphorylated CDK2 wt - human cyclin A3 complex with ATP”. X-ray diffraction, 2 ligands (ATP, MG), 12 pockets (best druggability 0.81). MolNFT v1 #90621 on GenesisL1: 3D structure, binding sites…
- PDB
- 4EOQ
- Type
- protein
- Length
- 1,083 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyclin-dependent kinase 2; Cyclin-A2
- EC
- 2.7.11.22
- UniProt
- P24941, P20248
- Ligands
- ATP, MG
- Pockets
- 12 · best druggability 0.81
Structure
x-ray diffraction · 4 distinct chains · 51% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cyclin-dependent kinase 2 (EC 2.7.11.22) | protein | 296 | 35% helix, 17% strand | P24941 |
| B | Cyclin-A2 | protein | 257 | 70% helix, 0% strand | P20248 |
| C | Cyclin-dependent kinase 2 (EC 2.7.11.22) | protein | 276 | 36% helix, 18% strand | P24941 |
| D | Cyclin-A2 | protein | 254 | 68% helix, 0% strand | P20248 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 2 copies · chains A, C
- MG · Magnesium ion · metal · 2 copies · chains A, B
- SGM · Monothioglycerol · additive · 2 copies · chains B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 124 | 0.81 | 0.99 | 23 | empty |
| 2 | 113 | 0.79 | 0.98 | 20 | empty |
| 3 | 1045 | 0.79 | 0.80 | 117 | empty |
| 4 | 307 | 0.68 | 0.82 | 39 | ATP, MG |
| 5 | 330 | 0.66 | 0.81 | 37 | ATP |
Interfaces
5 interfaces between chains.
- C–D · 1689 Ų buried · 28 hydrogen bonds · protein-protein
- A–B · 1604 Ų buried · 27 hydrogen bonds · protein-protein
- B–C · 576 Ų buried · 1 hydrogen bond · protein-protein
- A–D · 496 Ų buried · 2 hydrogen bonds · protein-protein
- A–C · 75 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent, 2 modified (additive adduct, phosphorylation).
Compared structures
- 4EOQ · Thr 160 phosphorylated CDK2 WT - human cyclin A3 complex with ATP · 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 B against A, TM-score 1.00
- 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
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P24941
- Every structure of UniProt P20248
- Elsewhere: RCSB PDB 4EOQ · PDBe 4EOQ · UniProt P24941 · UniProt P20248
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