Research workbench
Crystal structure of mdmx phosporylated TYR99 in complex with a 12-mer peptide
Analyse Crystal structure of mdmx phosporylated TYR99 in complex with a 12-mer peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4RXZ
- Type
- protein
- Length
- 189 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein MDM4; 12-mer peptide inhibitor
- UniProt
- O15151
- Pockets
- 1 · best druggability 0.57
Structure
x-ray diffraction · 3 distinct chains · 47% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protein MDM4 | protein | 84 | 46% helix, 15% strand | O15151 |
| C | 12-mer peptide inhibitor | protein | 11 | 45% helix, 0% strand | — |
| D | 12-mer peptide inhibitor | protein | 10 | 50% helix, 0% strand | — |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 252 | 0.57 | 0.78 | 35 | empty |
Interfaces
5 interfaces between chains.
- A–C · 498 Ų buried · 3 hydrogen bonds · protein-protein
- B–D · 483 Ų buried · 2 hydrogen bonds · protein-protein
- A–B · 294 Ų buried · 8 hydrogen bonds · protein-protein
- A–D · 84 Ų buried · 0 hydrogen bonds · protein-protein
- C–B · 76 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 4RXZ · Crystal Structure of MDMX phosporylated Tyr99 in complex with a 12-mer peptide · the same entry in another collection · chain B against B, TM-score 1.00
- O15151 · AlphaFold monomer V2.0 prediction for protein MDM4 (O15151) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 4RXZ · PDBe 4RXZ · UniProt O15151
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