Research workbench
Structure of human MDM2 in complex with an optimized P53 peptide
Analyse Structure of human MDM2 in complex with an optimized P53 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1T4F
- Type
- protein
- Length
- 97 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ubiquitin-protein ligase E3 MDM2; Optimized P53 peptide
- EC
- 6.3.2.-
- UniProt
- Q00987
- Ligands
- SO4
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| M | Ubiquitin-protein ligase E3 MDM2 (EC 6.3.2.-) | protein | 88 | 44% helix, 23% strand | Q00987 |
| P | Optimized P53 peptide | protein | 9 | 56% helix, 0% strand | — |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains M
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- M–P · 545 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 1T4F · Structure of human MDM2 in complex with an optimized p53 peptide · the same entry in another collection · chain M against M, TM-score 1.00
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 Q00987
- Elsewhere: RCSB PDB 1T4F · PDBe 1T4F · UniProt Q00987
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