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Canonical POLY(ADP-ribose) glycohydrolase from tetrahymena thermophila.

Analyse Canonical POLY(ADP-ribose) glycohydrolase from tetrahymena thermophila. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4EPP
Type: protein
Length: 878 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: POLY(ADP-ribose) glycohydrolase
Ligands: APR
Pockets: 6 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	POLY(ADP-ribose) glycohydrolase	protein	439	46% helix, 16% strand	—

Ligands and binding sites

APR · Adenosine-5-diphosphoribose · ligand · 2 copies · chains A, B

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

Pockets

6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	233	0.67	0.84	39	APR
2	189	0.66	0.85	33	APR
3	286	0.56	0.77	28	empty
4	316	0.55	0.75	32	empty
5	71	0.34	0.76	14	empty

Interfaces

1 interface between chains.

A–B · 290 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

4EPP · Canonical poly(ADP-ribose) glycohydrolase from Tetrahymena thermophila. · 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
Elsewhere: RCSB PDB 4EPP · PDBe 4EPP

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