MolNFT v1 · #100860 · protein

Crystal structure of mouse POLY(ADP-ribose) glycohydrolase (parg) catalytic domain mutant E748N

4NA5: “Crystal structure of mouse POLY(ADP-ribose) glycohydrolase (parg) catalytic domain mutant E748N”. X-ray diffraction, 1 ligand (SO4), 3 pockets (best druggability 0.70). MolNFT v1 #100860 on GenesisL1: 3D structure, binding sites and…

PDB: 4NA5
Type: protein
Length: 505 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: POLY(ADP-ribose) glycohydrolase
EC: 3.2.1.143
UniProt: O88622
Ligands: SO4
Pockets: 3 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	POLY(ADP-ribose) glycohydrolase (EC 3.2.1.143)	protein	505	39% helix, 15% strand	O88622

Ligands and binding sites

SO4 · Sulfate ion · ion · 4 copies · chains A

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	417	0.70	0.81	42	empty
2	155	0.53	0.80	22	empty
3	112	0.47	0.79	19	empty

Compared structures

4NA5 · Crystal structure of mouse poly(ADP-ribose) glycohydrolase (PARG) catalytic domain mutant… · the same entry in another collection · chain A against A, TM-score 1.00
O88622 · AlphaFold monomer V2.0 prediction for POLY(ADP-ribose) glycohydrolase (O88622) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 O88622
Elsewhere: RCSB PDB 4NA5 · PDBe 4NA5 · UniProt O88622

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