Research workbench
Human ARTD3 (PARP3) - catalytic domain in complex with inhibitor STO1542
Analyse Human ARTD3 (PARP3) - catalytic domain in complex with inhibitor STO1542 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4L7O
- Type
- protein
- Length
- 354 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Poly [ADP-ribose] polymerase 3
- EC
- 2.4.2.30
- UniProt
- Q9Y6F1
- Ligands
- 1VD
- Pockets
- 3 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Poly [ADP-ribose] polymerase 3 (EC 2.4.2.30) | protein | 354 | 37% helix, 23% strand | Q9Y6F1 |
Ligands and binding sites
- 1VD · N-{(1S)-1-[4-(1H-imidazol-1-yl)phenyl]ethyl}-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide · ligand · chains A
- DMS · Dimethyl sulfoxide · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 478 | 0.74 | 0.83 | 45 | 1VD, DMS |
| 2 | 87 | 0.34 | 0.74 | 20 | empty |
| 3 | 53 | 0.28 | 0.75 | 14 | empty |
Compared structures
- 4L7O · Human artd3 (parp3) - catalytic domain in complex with inhibitor STO1542 · the same entry in another collection · chain A against A, TM-score 1.00
- Q9Y6F1 · AlphaFold monomer V2.0 prediction for protein mono-ADP- ribosyltransferase PARP3 (Q9Y6F1) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q9Y6F1
- Elsewhere: RCSB PDB 4L7O · PDBe 4L7O · UniProt Q9Y6F1
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