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The X-ray crystal structure of POLY(ADP-ribose) glycohydrolase bound to the inhibitor ADP-hpd from thermomonospora curvata

Analyse The X-ray crystal structure of POLY(ADP-ribose) glycohydrolase bound to the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3SII
Type: protein
Length: 265 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: D1AC29
Ligands: A1R
Pockets: 1 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	POLY(ADP-ribose) glycohydrolase (EC 3.2.1.143)	protein	265	45% helix, 20% strand	D1AC29

Ligands and binding sites

A1R · 5'-O-[(S)-{[(S)-{[(2R,3R,4S)-3,4-dihydroxypyrrolidin-2-yl]methoxy}(hydroxy)phosphoryl]oxy}(hydroxy) phosphoryl]adenosine · 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	384	0.70	0.82	48	A1R

Compared structures

3SII · The X-ray crystal structure of poly(ADP-ribose) glycohydrolase bound to the inhibitor… · 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 D1AC29
Elsewhere: RCSB PDB 3SII · PDBe 3SII · UniProt D1AC29

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