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Structure of human PARP1 catalytic domain bound to a quinazoline-2, 4(1H,3H)-dione inhibitor
Analyse Structure of human PARP1 catalytic domain bound to a quinazoline-2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5WRQ
- Type
- protein
- Length
- 702 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Poly [ADP-ribose] polymerase 1
- EC
- 2.4.2.30
- UniProt
- P09874
- Ligands
- 7TX
- Pockets
- 6 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Poly [ADP-ribose] polymerase 1 (EC 2.4.2.30) | protein | 351 | 38% helix, 24% strand | P09874 |
Ligands and binding sites
- 7TX · 5-[[2,4-bis(oxidanylidene)quinazolin-1-yl]methyl]-2-fluoranyl-N-[(3R)-1-(3-methylbutyl)pyrrolidin-3-yl]benzamide · ligand · 2 copies · chains A, 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 753 | 0.82 | 0.85 | 75 | 7TX |
| 2 | 435 | 0.80 | 0.88 | 45 | 7TX |
| 3 | 84 | 0.49 | 0.83 | 19 | empty |
| 4 | 59 | 0.48 | 0.85 | 17 | empty |
| 5 | 138 | 0.47 | 0.78 | 33 | empty |
Interfaces
1 interface between chains.
- A–B · 852 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 5WRQ · Structure of human PARP1 catalytic domain bound to a quinazoline-2,4(1H,3H)-dione… · 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 P09874
- Elsewhere: RCSB PDB 5WRQ · PDBe 5WRQ · UniProt P09874
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