Research workbench
Human PARP14 (ARTD8), catalytic fragment in complex with an N-aryl piperazine inhibitor
Analyse Human PARP14 (ARTD8), catalytic fragment in complex with an N-aryl piperazine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5NQE
- Type
- protein
- Length
- 360 residues
- Chains
- 2
- 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
- 94Z
- Pockets
- 1 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 22% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Poly [ADP-ribose] polymerase 14 (EC 2.4.2.30) | protein | 180 | 22% helix, 34% strand | Q460N5 |
Ligands and binding sites
- 94Z · 3-[[4-[4-(4-fluorophenyl)piperazin-1-yl]-4-oxidanylidene-butanoyl]amino]benzamide · ligand · 2 copies · chains A, B
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.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 894 | 0.71 | 0.76 | 76 | 94Z |
Interfaces
1 interface between chains.
- A–B · 175 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 5NQE · Human PARP14 (ARTD8), catalytic fragment in complex with an N-aryl piperazine 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 0.95
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 5NQE · PDBe 5NQE · UniProt Q460N5
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