Research workbench

Crystal structure of POLY(ADP-ribose) glycohydrolase (parg) T267K mutant from deinococcus radiodurans in complex with ADP-ribose

Analyse Crystal structure of POLY(ADP-ribose) glycohydrolase (parg) T267K mutant from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5ZDF
Type: protein
Length: 248 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Poly ADP-ribose glycohydrolase
UniProt: Q9RZM4
Ligands: AR6
Pockets: 1 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Poly ADP-ribose glycohydrolase	protein	248	44% helix, 19% strand	Q9RZM4

Ligands and binding sites

AR6 · [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxy-oxolan-2-yl]methyl [hydroxy-[[(2R,3S,4R,5S)-3,4,5-trihydroxyoxolan-2-yl]methoxy]phosphoryl] hydrogen phosphate · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	317	0.68	0.82	48	AR6

Compared structures

5ZDF · Crystal structure of poly(ADP-ribose) glycohydrolase (PARG) T267K mutant from Deinococcus… · 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 Q9RZM4
Elsewhere: RCSB PDB 5ZDF · PDBe 5ZDF · UniProt Q9RZM4

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.