MolNFT v1 · #177523 · protein
The crystal structure of P53P peptide fragment in complex with the N- terminal domain of mdmx
7EL4 · Cellular tumor antigen P53,PROTEIN MDM4: “The crystal structure of P53P peptide fragment in complex with the N- terminal domain of mdmx”. X-ray diffraction, 2 ligands (O4B, MG). MolNFT v1 #177523 on GenesisL1: 3D structure, binding…
- PDB
- 7EL4
- Type
- protein
- Length
- 94 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cellular tumor antigen P53,PROTEIN MDM4
- UniProt
- P04637, O15151
- Ligands
- O4B, MG
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cellular tumor antigen P53,PROTEIN MDM4 | protein | 94 | 47% helix, 15% strand | P04637, O15151 |
Ligands and binding sites
- O4B · 1,4,7,10,13,16-hexaoxacyclooctadecane · ligand · 2 copies · chains A
- MG · Magnesium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7EL4 · The crystal structure of p53p peptide fragment in complex with the N-terminal domain of… · the same entry in another collection · chain A against A, 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 0.87
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 P04637
- Every structure of UniProt O15151
- Elsewhere: RCSB PDB 7EL4 · PDBe 7EL4 · UniProt P04637 · UniProt O15151
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