Research workbench
PARP15 catalytic domain in complex with OUL242
Analyse PARP15 catalytic domain in complex with OUL242 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7PX7
- Type
- protein
- Length
- 393 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein mono-ADP-ribosyltransferase PARP15
- EC
- 2.4.2.-
- UniProt
- Q460N3
- Ligands
- 8DB
- Pockets
- 5 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 24% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein mono-ADP-ribosyltransferase PARP15 (EC 2.4.2.-) | protein | 195 | 24% helix, 30% strand | Q460N3 |
| B | Protein mono-ADP-ribosyltransferase PARP15 (EC 2.4.2.-) | protein | 198 | 25% helix, 29% strand | Q460N3 |
Ligands and binding sites
- 8DB · 6-(thiophen-2-ylmethoxy)phthalazine-1,4-dione · ligand · chains A
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 252 | 0.79 | 0.92 | 44 | empty |
| 2 | 269 | 0.76 | 0.88 | 26 | empty |
| 3 | 277 | 0.63 | 0.80 | 32 | 8DB, MPD |
| 4 | 227 | 0.62 | 0.81 | 35 | empty |
| 5 | 70 | 0.34 | 0.76 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1089 Ų buried · 21 hydrogen bonds · protein-protein
Compared structures
- 7PX7 · PARP15 catalytic domain in complex with OUL242 · 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 Q460N3
- Elsewhere: RCSB PDB 7PX7 · PDBe 7PX7 · UniProt Q460N3
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