Research workbench
PARP15 catalytic domain in complex with OUL240
Analyse PARP15 catalytic domain in complex with OUL240 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7PWQ
- 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
- 8A8
- Pockets
- 5 · best druggability 0.80
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 | 24% helix, 29% strand | Q460N3 |
Ligands and binding sites
- 8A8 · 6-(cyclohexylmethoxy)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 | 250 | 0.80 | 0.93 | 43 | empty |
| 2 | 255 | 0.75 | 0.89 | 30 | empty |
| 3 | 213 | 0.63 | 0.83 | 26 | empty |
| 4 | 274 | 0.63 | 0.81 | 33 | 8A8, MPD |
| 5 | 79 | 0.34 | 0.75 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1096 Ų buried · 21 hydrogen bonds · protein-protein
Compared structures
- 7PWQ · PARP15 catalytic domain in complex with OUL240 · 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 7PWQ · PDBe 7PWQ · UniProt Q460N3
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