Research workbench
PARP15 catalytic domain in complex with OUL221
Analyse PARP15 catalytic domain in complex with OUL221 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7PWP
- Type
- protein
- Length
- 392 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
- 8BE
- Pockets
- 5 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 23% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein mono-ADP-ribosyltransferase PARP15 (EC 2.4.2.-) | protein | 194 | 24% helix, 33% strand | Q460N3 |
| B | Protein mono-ADP-ribosyltransferase PARP15 (EC 2.4.2.-) | protein | 198 | 23% helix, 29% strand | Q460N3 |
Ligands and binding sites
- 8BE · 4-[(3-bromophenyl)methoxy]-2-methoxy-benzamide · ligand · chains A
- DMS · Dimethyl sulfoxide · additive · chains B
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 | 255 | 0.80 | 0.92 | 44 | empty |
| 2 | 256 | 0.76 | 0.89 | 29 | empty |
| 3 | 215 | 0.60 | 0.81 | 36 | DMS |
| 4 | 279 | 0.57 | 0.77 | 37 | 8BE |
| 5 | 83 | 0.36 | 0.76 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1111 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 7PWP · PARP15 catalytic domain in complex with OUL221 · 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 7PWP · PDBe 7PWP · UniProt Q460N3
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.