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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: 2FP0
Type: protein
Length: 678 residues
Chains: 2
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 0.53

Structure

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

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

Ligands and binding sites

MG · Magnesium ion · metal · 4 copies · chains A, B

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	265	0.53	0.76	38	empty
2	142	0.48	0.78	29	MG
3	130	0.43	0.76	29	MG

Interfaces

1 interface between chains.

A–B · 486 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

2FP0 · 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 B 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 2FP0 · PDBe 2FP0 · UniProt Q9NX46

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