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HDM2 (17-111, wild type) complexed with compound 11 at 2.0A; structural states of HDM2 and hdmx: X-ray elucidation of adaptations and binding interactions for different chemical compound classes

Analyse HDM2 (17-111, wild type) complexed with compound 11 at 2.0A; structural states… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6Q9H
Type: protein
Length: 92 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: E3 ubiquitin-protein ligase MDM2
EC: 2.3.2.27
UniProt: Q00987
Ligands: HRH
Pockets: 1 · best druggability 0.47

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	E3 ubiquitin-protein ligase MDM2 (EC 2.3.2.27)	protein	92	48% helix, 16% strand	Q00987

Ligands and binding sites

HRH · (4~{S})-5-(3-chloranyl-2-fluoranyl-phenyl)-4-(4-chloranyl-2-methyl-phenyl)-3-propan-2-yl-1,4-dihydropyrrolo[3,4-c]pyrazol-6-one · 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	119	0.47	0.78	15	HRH

Compared structures

6Q9H · HDM2 (17-111, WILD TYPE) COMPLEXED WITH COMPOUND 11 AT 2.0A; Structural states of Hdm2… · 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 6Q9H · PDBe 6Q9H · UniProt Q00987

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