Research workbench
PARP15 catalytic domain in complex with OUL113
Analyse PARP15 catalytic domain in complex with OUL113 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7OSP
- 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
- 0Q6
- Pockets
- 6 · best druggability 0.77
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 | 194 | 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
- 0Q6 · 4-[(3-bromophenyl)methoxy]benzamide · ligand · chains A
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains A
- DMS · Dimethyl sulfoxide · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 257 | 0.77 | 0.90 | 37 | empty |
| 2 | 209 | 0.77 | 0.92 | 41 | empty |
| 3 | 174 | 0.61 | 0.83 | 26 | DMS |
| 4 | 231 | 0.57 | 0.79 | 30 | 0Q6, MPD |
| 5 | 69 | 0.33 | 0.75 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1107 Ų buried · 22 hydrogen bonds · protein-protein
Compared structures
- 7OSP · PARP15 catalytic domain in complex with OUL113 · 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 7OSP · PDBe 7OSP · UniProt Q460N3
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