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Crystal structure analysis of zebra fish mdmx
Analyse Crystal structure analysis of zebra fish mdmx in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6V4G
- Type
- protein
- Length
- 103 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein MDM4; Stapled peptide QSQQTF(0EH)NLWRLE(MK8)QN(NH2)
- UniProt
- Q7ZUW7
- Ligands
- 0EH, NH2, SO4
- Pockets
- 1 · best druggability 0.33
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein MDM4 | protein | 90 | 44% helix, 18% strand | Q7ZUW7 |
| B | Stapled peptide QSQQTF(0EH)NLWRLE(MK8)QN(NH2) | protein | 13 | 46% helix, 0% strand | — |
Ligands and binding sites
- 0EH · (2R)-2-amino-2-methylnonanoic acid · ligand · chains A, B
- NH2 · Amino group · ion · chains B
- SO4 · Sulfate ion · ion · chains A
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 | 58 | 0.33 | 0.77 | 12 | 0EH |
Interfaces
1 interface between chains.
- A–B · 536 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 covalent, 1 modified (covalent ligand, nonstandard).
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 Q7ZUW7
- Elsewhere: RCSB PDB 6V4G · PDBe 6V4G · UniProt Q7ZUW7
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