Research workbench
Xenopus laevis MDM2 bound to the transactivation domain of human P53
Analyse Xenopus laevis MDM2 bound to the transactivation domain of human P53 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1YCQ
- Type
- protein
- Length
- 99 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- MDM2; P53
- UniProt
- P56273, P04637
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | MDM2 | protein | 88 | 44% helix, 16% strand | P56273 |
| B | P53 | protein | 11 | 45% helix, 0% strand | P04637 |
Interfaces
1 interface between chains.
- A–B · 523 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 1YCQ · Xenopus laevis MDM2 bound to the transactivation domain of human P53 · the same entry in another collection · chain A against A, TM-score 1.00
- P56273 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase MDM2 (P56273) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P56273
- Every structure of UniProt P04637
- Elsewhere: RCSB PDB 1YCQ · PDBe 1YCQ · UniProt P56273 · UniProt P04637
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