Research workbench
Structure of PARP2 catalytic domain bound to an isoindolinone inhibitor
Analyse Structure of PARP2 catalytic domain bound to an isoindolinone inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ZZX
- Type
- protein
- Length
- 700 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Poly [ADP-ribose] polymerase 2
- EC
- 2.4.2.30
- UniProt
- Q9UGN5
- Ligands
- FSU
- Pockets
- 5 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Poly [ADP-ribose] polymerase 2 (EC 2.4.2.30) | protein | 351 | 38% helix, 24% strand | Q9UGN5 |
| B | Poly [ADP-ribose] polymerase 2 (EC 2.4.2.30) | protein | 349 | 38% helix, 24% strand | Q9UGN5 |
Ligands and binding sites
- FSU · 2-(3-methoxypropyl)-3-oxo-2,3-dihydro-1H-isoindole-4-carboxamide · ligand · 2 copies · chains A, 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, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 659 | 0.77 | 0.82 | 57 | FSU |
| 2 | 622 | 0.77 | 0.82 | 57 | FSU |
| 3 | 207 | 0.55 | 0.78 | 35 | empty |
| 4 | 116 | 0.49 | 0.80 | 23 | empty |
| 5 | 69 | 0.32 | 0.75 | 16 | empty |
Compared structures
- 4ZZX · Structure of PARP2 catalytic domain bound to an isoindoli inhibitor · the same entry in another collection · chain A against A, TM-score 1.00
- Q9UGN5 · AlphaFold monomer V2.0 prediction for poly [ADP-ribose] polymerase 2 (Q9UGN5) · a predicted model of the same protein · chain B 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 Q9UGN5
- Elsewhere: RCSB PDB 4ZZX · PDBe 4ZZX · UniProt Q9UGN5
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