Research workbench
CDK2/CYCLIN a in complex with a 9 residue recruitment peptide from E2F
Analyse CDK2/CYCLIN a in complex with a 9 residue recruitment peptide from E2F in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1H24
- Type
- protein
- Length
- 1,113 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P24941, P20248, Q01094
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 294 | — | P24941 |
| B, D | — | protein | 258 | — | P20248 |
| E | — | protein | 9 | — | Q01094 |
Compared structures
- 1H24 · CDK2/CyclinA in complex with a 9 residue recruitment peptide from E2F · 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
- Q01094 · AlphaFold monomer V2.0 prediction for transcription factor E2F1 (Q01094) · a predicted model of the same protein · chain E against A, TM-score 0.39
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 Q01094
- Elsewhere: RCSB PDB 1H24 · PDBe 1H24 · UniProt P24941 · UniProt P20248 · UniProt Q01094
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