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Crystal structure of PARP14 bound to N-{4-[4-(diphenylmethoxy) piperidin-1-YL]BUTYL}[1,2,4]TRIAZOLO[4,3-B]PYRIDAZIN-6-amine inhibitor

Analyse Crystal structure of PARP14 bound to N-{4-[4-(diphenylmethoxy)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5V7T
Type: protein
Length: 173 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: 91V
Pockets: 1 · best druggability 0.33

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Poly [ADP-ribose] polymerase 14 (EC 2.4.2.30)	protein	173	26% helix, 31% strand	Q460N5

Ligands and binding sites

91V · N-{4-[4-(diphenylmethoxy)piperidin-1-yl]butyl}[1,2, 4]triazolo[4,3-b]pyridazin-6-amine · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	50	0.33	0.78	16	empty

Compared structures

5V7T · crystal structure of PARP14 bound to N-{4-[4-(diphenylmethoxy)piperidin-1-yl]butyl}[1,2,4]… · 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 Q460N5
Elsewhere: RCSB PDB 5V7T · PDBe 5V7T · UniProt Q460N5

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