Research workbench
Human PARP14 (ARTD8), catalytic fragment in complex with RBN012759
Analyse Human PARP14 (ARTD8), catalytic fragment in complex with RBN012759 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6WE2
- Type
- protein
- Length
- 369 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Isoform 1 of protein mono-ADP-ribosyltransferase PARP14
- EC
- 2.4.2.-
- UniProt
- Q460N5
- Ligands
- XBA
- Pockets
- 4 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 23% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Isoform 1 of protein mono-ADP-ribosyltransferase PARP14 (EC 2.4.2.-) | protein | 189 | 23% helix, 33% strand | Q460N5 |
| B | Isoform 1 of protein mono-ADP-ribosyltransferase PARP14 (EC 2.4.2.-) | protein | 180 | 24% helix, 30% strand | Q460N5 |
Ligands and binding sites
- XBA · 7-(cyclopropylmethoxy)-5-fluoro-2-{[(trans-4-hydroxycyclohexyl)sulfanyl]methyl}quinazolin-4(3H)-one · ligand · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 570 | 0.81 | 0.86 | 62 | XBA |
| 2 | 82 | 0.33 | 0.74 | 19 | empty |
| 3 | 61 | 0.32 | 0.76 | 14 | empty |
| 4 | 53 | 0.28 | 0.74 | 11 | empty |
Interfaces
1 interface between chains.
- A–B · 737 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 6WE2 · Human PARP14 (ARTD8), catalytic fragment in complex with RBN012759 · 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 6WE2 · PDBe 6WE2 · UniProt Q460N5
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.