- PDB-4a0d: Structure of unliganded human PARG catalytic domain -
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Open data
ID or keywords:
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Basic information
Entry
Database: PDB / ID: 4a0d
Title
Structure of unliganded human PARG catalytic domain
Components
POLY(ADP-RIBOSE) GLYCOHYDROLASE
Keywords
HYDROLASE
Function / homology
Function and homology information
nucleotide-sugar metabolic process / poly(ADP-ribose) glycohydrolase / poly(ADP-ribose) glycohydrolase activity / ATP generation from poly-ADP-D-ribose / POLB-Dependent Long Patch Base Excision Repair / regulation of DNA repair / base-excision repair, gap-filling / carbohydrate metabolic process / nuclear body / mitochondrial matrix ...nucleotide-sugar metabolic process / poly(ADP-ribose) glycohydrolase / poly(ADP-ribose) glycohydrolase activity / ATP generation from poly-ADP-D-ribose / POLB-Dependent Long Patch Base Excision Repair / regulation of DNA repair / base-excision repair, gap-filling / carbohydrate metabolic process / nuclear body / mitochondrial matrix / nucleoplasm / nucleus / cytosol / cytoplasm Similarity search - Function
Mass: 18.015 Da / Num. of mol.: 411 / Source method: isolated from a natural source / Formula: H2O
Compound details
ENGINEERED RESIDUE IN CHAIN A, LYS 616 TO ALA ENGINEERED RESIDUE IN CHAIN A, GLN 617 TO ALA ...ENGINEERED RESIDUE IN CHAIN A, LYS 616 TO ALA ENGINEERED RESIDUE IN CHAIN A, GLN 617 TO ALA ENGINEERED RESIDUE IN CHAIN A, LYS 618 TO ALA ENGINEERED RESIDUE IN CHAIN A, GLU 688 TO ALA ENGINEERED RESIDUE IN CHAIN A, LYS 689 TO ALA ENGINEERED RESIDUE IN CHAIN A, LYS 690 TO ALA
Sequence details
SIX MUTATIONS INTRODUCED TO IMPROVE CRYSTALLISABILITY K617A,Q618A,K619A,E688A,K689A,K690A
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Experimental details
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Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
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Sample preparation
Crystal
Density Matthews: 2.49 Å3/Da / Density % sol: 50.54 % Description: STRUCTURE SOLVED BY MOLECULAR REPLACEMENT USING COORDINATES FROM SEMET MAD DETERMINATION IN ALTERNATIVE SPACE GROUP