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PARP14 macrodomain 2 with inhibitor

Analyse PARP14 macrodomain 2 with inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5O2D
Type: protein
Length: 189 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Poly [ADP-ribose] polymerase 14
EC: 2.4.2.30
UniProt: Q460N5
Ligands: 9HH
Pockets: 2 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Poly [ADP-ribose] polymerase 14 (EC 2.4.2.30)	protein	189	40% helix, 18% strand	Q460N5

Ligands and binding sites

9HH · ~{N}-[2-(9~{H}-carbazol-1-yl)phenyl]methanesulfonamide · ligand · chains A

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

Pockets

2 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	168	0.82	0.97	25	9HH
2	142	0.47	0.78	24	empty

Compared structures

5O2D · PARP14 Macrodomain 2 with inhibitor · the same entry in another collection · chain A against A, TM-score 1.00
Q460N5 · AlphaFold monomer V2.0 prediction for protein mono-ADP- ribosyltransferase PARP14 (Q460N5) · a predicted model of the same protein · chain A against A, TM-score 0.94

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 Q460N5
Elsewhere: RCSB PDB 5O2D · PDBe 5O2D · UniProt Q460N5

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