Brand  (β version)

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
SO4 Sulfate ion
CL Chloride ion
Non-standard Residues
Code Name Show
DSG D-asparagine
DTR D-tryptophan
DTY D-tyrosine
DAL D-alanine
DLE D-leucine
DGL D-glutamic acid
DLY D-lysine
DAR D-arginine
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 3LNJ   PDBj   RCSB PDB   PDBe
Header : LIGASE/LIGASE INHIBITOR
Title : Crystal structure of human MDM2 in complex with D-peptide inhibitor (DPMI-alpha)
Release Data : 2010-03-09
Compound :
mol_id molecule chains synonym
1 E3 ubiquitin-protein ligase Mdm2 A,C,E p53-binding protein Mdm2, Oncoprotein Mdm2, Double minute 2 protein, Hdm2
ec: 6.3.2.-
fragment: UNP residues 25-109, P53 BINDING DOMAIN
mol_id molecule chains
2 D-peptide inhibitor B,D,F
Source :
mol_id organism_scientific
1
synthetic: yes
other_details: MDM2 sequence occurs naturally in humans.
mol_id organism_scientific
2
synthetic: yes
other_details: Synthetic peptide, D-enantiomer of phage-selected L-peptide
Authors : Pazgier, M., Lu, W.
Keywords : MDM2, p53 binding domain, D-peptide activator of MDM2, MDM2-D-peptide complex, Host-virus interaction, Ligase, Metal-binding, Nucleus, Phosphoprotein, Proto-oncogene, Ubl conjugation pathway, Zinc-finger, LIGASE-LIGASE INHIBITOR complex
Exp. method : X-RAY DIFFRACTION ( 2.40 Å )
Citation :

A left-handed solution to peptide inhibition of the p53-MDM2 interaction.

Liu, M.,Pazgier, M.,Li, C.  et al.
(2010)  Angew.Chem.Int.Ed.Engl.  49 : 3649 - 3652

PubMed: 20449836
DOI: 10.1002/anie.201000329

Chain : A, C, E
UniProt : Q00987 (MDM2_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine. 2.3.2.27 PubMed:12821780
-