MolNFT v1 · #164582 · protein

Multicomponent peptide stapling as a diversity-driven tool for the development of inhibitors of protein-protein interactions

6T2F · E3 ubiquitin-protein ligase MDM2: “Multicomponent peptide stapling as a diversity-driven tool for the development of inhibitors of…”. X-ray diffraction, 1 ligand (M9H). MolNFT v1 #164582 on GenesisL1: 3D structure, binding sites and…

PDB: 6T2F
Type: protein
Length: 99 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: E3 ubiquitin-protein ligase MDM2; MDM2 in complex with GAR300-am
EC: 2.3.2.27
UniProt: Q00987
Ligands: M9H

Structure

x-ray diffraction · 2 distinct chains · 46% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	E3 ubiquitin-protein ligase MDM2 (EC 2.3.2.27)	protein	85	44% helix, 13% strand	Q00987
B	MDM2 in complex with GAR300-am	protein	14	64% helix, 0% strand	—

Ligands and binding sites

M9H · 2-(methylamino)-~{N}-[[3-[[2-(methylamino) ethanoylamino]methyl]phenyl]methyl]ethanamide · ligand · 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 · 675 Å² buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 covalent (covalent ligand).

Compared structures

6T2F · Multicomponent Peptide Stapling as a Diversity-Driven Tool for the Development of… · the same entry in another collection · chain A against A, TM-score 1.00

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 Q00987
Elsewhere: RCSB PDB 6T2F · PDBe 6T2F · UniProt Q00987

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