MolNFT v1 · #63588 · protein
Crystal structure of hdmx bound to the P53-peptidomimetic ac-phe-met- aib-pmp-TRP-glu-AC3C-leu-NH2 at 1.35A
3FE7 · MDM4 protein: “Crystal structure of hdmx bound to the P53-peptidomimetic ac-phe-met- aib-pmp-TRP-glu-AC3C-leu-NH2 at 1.35A”. X-ray diffraction, 2 ligands (ACE, NH2). MolNFT v1 #63588 on GenesisL1: 3D structure, binding sites and…
- PDB
- 3FE7
- Type
- protein
- Length
- 91 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- MDM4 protein; P53-peptidomimetic ac-phe-met-aib-pmp-TRP-glu-AC3C-leu-NH2
- UniProt
- O15151
- Ligands
- ACE, NH2
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | MDM4 protein | protein | 83 | 47% helix, 20% strand | O15151 |
| L | P53-peptidomimetic ac-phe-met-aib-pmp-TRP-glu-AC3C-leu-NH2 | protein | 8 | 50% helix, 0% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–L · 478 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified, 1 covalent (nonstandard, covalent ligand).
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 3FE7 · PDBe 3FE7 · UniProt O15151
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