Research workbench
X-ray structure of HDM2/CMR19 at 1.45A: discovery, X-ray structure and cpp-conjugation enabled uptake of P53/MDM2 macrocyclic peptide inhibitors
Analyse X-ray structure of HDM2/CMR19 at 1.45A: discovery, X-ray structure and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7NUS
- Type
- protein
- Length
- 311 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q00987
- Ligands
- GM1, SO4, CL
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 86 | — | Q00987 |
| B | — | protein | 88 | — | Q00987 |
| C | — | protein | 95 | — | Q00987 |
| D, E, F | — | protein | 14 | — | — |
Ligands and binding sites
- GM1 · Aminomethylamide · ligand · 3 copies · chains A, D, B, E, C, F
- SO4 · Sulfate ion · ion · 2 copies · chains A
- CL · Chloride ion · ion · 2 copies · chains E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7NUS · X-RAY STRUCTURE OF HDM2/CMR19 AT 1.45A: Discovery, X-ray structure and CPP-conjugation… · the same entry in another collection · chain A against A, 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 7NUS · PDBe 7NUS · UniProt Q00987
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