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Structure of NUDT15 in complex with inhibitor TH8321

Analyse Structure of NUDT15 in complex with inhibitor TH8321 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7AOP
Type: protein
Length: 156 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Probable 8-oxo-dgtp diphosphatase NUDT15
EC: 3.6.1.9
UniProt: Q9NV35
Ligands: RTW, MG
Pockets: 1 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 20% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Probable 8-oxo-dgtp diphosphatase NUDT15 (EC 3.6.1.9)	protein	156	20% helix, 37% strand	Q9NV35

Ligands and binding sites

RTW · 2-azanyl-9-cyclohexyl-8-(2-methoxyphenyl)-3~{H}-purine-6-thione · ligand · chains A
MG · Magnesium ion · metal · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	285	0.68	0.83	36	RTW, MG

Compared structures

7AOP · Structure of NUDT15 in complex with inhibitor TH8321 · the same entry in another collection · chain A against A, TM-score 1.00
Q9NV35 · AlphaFold monomer V2.0 prediction for nucleotide triphosphate diphosphatase NUDT15… · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q9NV35
Elsewhere: RCSB PDB 7AOP · PDBe 7AOP · UniProt Q9NV35

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