Research workbench
Structure of human mdmx protein in complex with a small molecule inhibitor
Analyse Structure of human mdmx protein in complex with a small molecule inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3LBJ
- Type
- protein
- Length
- 83 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein MDM4
- UniProt
- O15151
- Ligands
- WW8, SO4
- Pockets
- 1 · best druggability 0.39
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | Protein MDM4 | protein | 83 | 46% helix, 19% strand | O15151 |
Ligands and binding sites
- WW8 · N-[(3S)-1-({6-chloro-3-[1-(4-chlorobenzyl)-4-phenyl-1H-imidazol-5-yl]-1H-indol-2-yl}carbonyl)pyrrolidin-3-yl]-N,N',N'-trimethylpropane-1,3-diamine · ligand · 2 copies · chains E
- SO4 · Sulfate ion · ion · chains E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 59 | 0.39 | 0.79 | 15 | empty |
Compared structures
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 O15151
- Elsewhere: RCSB PDB 3LBJ · PDBe 3LBJ · UniProt O15151
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