MolNFT v1 · #11645 · protein
P27(KIP1)/CYCLIN A/CDK2 complex
1JSU: “P27(KIP1)/CYCLIN A/CDK2 complex”. X-ray diffraction. MolNFT v1 #11645 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1JSU
- Type
- protein
- Length
- 613 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P24941, P20248, P46527
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 286 | — | P24941 |
| B | — | protein | 258 | — | P20248 |
| C | — | protein | 69 | — | P46527 |
Compared structures
- 1JSU · P27(KIP1)/CYCLIN A/CDK2 complex · the same entry in another collection · chain A against A, 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 0.88
- P46527 · AlphaFold monomer V2.0 prediction for cyclin-dependent kinase inhibitor 1B (P46527) · a predicted model of the same protein · chain C against A, TM-score 0.73
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 1JSU · PDBe 1JSU · UniProt P24941 · UniProt P20248 · UniProt P46527
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