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Structure of human MDMX in complex with high affinity peptide

Analyse Structure of human MDMX in complex with high affinity peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3FDO
Type: protein
Length: 102 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.4
Source: Homo sapiens; SYNTHETIC CONSTRUCT
Molecule: Protein Mdm4; Synthetic high affinity peptide
UniProt: O15151
Ligands: MG

Structure

x-ray diffraction · resolution 1.4 · 2 distinct chains · 44% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein Mdm4	protein	90	43% helix, 20% strand	O15151
B	Synthetic high affinity peptide	protein	12	50% helix, 0% strand	—

Ligands and binding sites

MG · Magnesium ion · metal · 5 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Interfaces

1 interface between chains.

A–B · 534 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

3FDO · Structure of human mdmx in complex with high affinity peptide · 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 0.94

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 3FDO · PDBe 3FDO · UniProt O15151

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