Research workbench

Human ADP-ribosylhydrolase 3

Analyse Human ADP-ribosylhydrolase 3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2FOZ
Type: protein
Length: 339 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ADP-ribosylhydrolase like 2
UniProt: Q9NX46
Ligands: MG
Pockets: 3 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 67% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ADP-ribosylhydrolase like 2	protein	339	67% helix, 1% strand	Q9NX46

Ligands and binding sites

MG · Magnesium ion · metal · 2 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	50	0.70	0.98	20	empty
2	127	0.48	0.79	34	empty
3	72	0.34	0.76	18	empty

Compared structures

2FOZ · human ADP-ribosylhydrolase 3 · the same entry in another collection · chain A against A, TM-score 1.00
Q9NX46 · AlphaFold monomer V2.0 prediction for ADP-ribose glycohydrolase ARH3 (Q9NX46) · 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 Q9NX46
Elsewhere: RCSB PDB 2FOZ · PDBe 2FOZ · UniProt Q9NX46

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