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X-ray structure of the P53-MDM2 inhibitor NMI801 bound to HDM2 at 2.1A resolution

Analyse X-ray structure of the P53-MDM2 inhibitor NMI801 bound to HDM2 at 2.1A… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6I29
Type: protein
Length: 93 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Human E3 ubiquitin-protein ligase MDM2
UniProt: Q00987
Ligands: H0W
Pockets: 1 · best druggability 0.44

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Human E3 ubiquitin-protein ligase MDM2	protein	93	43% helix, 12% strand	Q00987

Ligands and binding sites

H0W · 6-chloranyl-3-[3-[(1~{S})-1-(4-chlorophenyl)ethyl]-5-phenyl-imidazol-4-yl]-~{N}-[2-[4-(2-oxidanylidene-1,3-oxazinan-3-yl)piperidin-1-yl]pyridin-3-yl]-1~{H}-indole-2-carboxamide · ligand · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	105	0.44	0.77	16	H0W

Compared structures

6I29 · X-ray structure of the p53-MDM2 inhibitor NMI801 bound to HDM2 at 2.1A resolution · 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 6I29 · PDBe 6I29 · UniProt Q00987

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