MolNFT v1 · #8483 · protein
CDK2/CYCLIN a in complex with an 11-residue recruitment peptide from P27
1H27 · Cell division protein kinase 2: “CDK2/CYCLIN a in complex with an 11-residue recruitment peptide from P27”. X-ray diffraction, 15 pockets (best druggability 0.80). MolNFT v1 #8483 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1H27
- Type
- protein
- Length
- 1,111 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cell division protein kinase 2; Cyclin A2; Cyclin-dependent kinase inhibitor 1B
- EC
- 2.7.1.-
- UniProt
- P24941, P20248, P46527
- Pockets
- 15 · best druggability 0.80
Structure
x-ray diffraction · 4 distinct chains · 45% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cell division protein kinase 2 (EC 2.7.1.-) | protein | 297 | 35% helix, 17% strand | P24941 |
| B, D | Cyclin A2 | protein | 258 | 69% helix, 0% strand | P20248 |
| C | Cell division protein kinase 2 (EC 2.7.1.-) | protein | 292 | 36% helix, 17% strand | P24941 |
| E | Cyclin-dependent kinase inhibitor 1B | protein | 6 | 0% helix, 0% strand | P46527 |
Pockets
15 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 124 | 0.80 | 0.98 | 23 | empty |
| 2 | 96 | 0.79 | 0.99 | 23 | empty |
| 3 | 1048 | 0.79 | 0.80 | 107 | empty |
| 4 | 278 | 0.70 | 0.84 | 38 | empty |
| 5 | 302 | 0.69 | 0.83 | 37 | empty |
Interfaces
6 interfaces between chains.
- C–D · 1790 Ų buried · 29 hydrogen bonds · protein-protein
- A–B · 1756 Ų buried · 35 hydrogen bonds · protein-protein
- B–C · 481 Ų buried · 1 hydrogen bond · protein-protein
- A–D · 457 Ų buried · 3 hydrogen bonds · protein-protein
- B–E · 394 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 1H27 · CDK2/CyclinA in complex with an 11-residue recruitment peptide from p27 · the same entry in another collection · chain E against E, 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
- P46527 · AlphaFold monomer V2.0 prediction for cyclin-dependent kinase inhibitor 1B (P46527) · a predicted model of the same protein · chain E against A, TM-score 0.46
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
- Every structure of UniProt P46527
- Elsewhere: RCSB PDB 1H27 · PDBe 1H27 · UniProt P24941 · UniProt P20248 · UniProt P46527
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