Research workbench
PARP15 catalytic domain in complex with OUL252
Analyse PARP15 catalytic domain in complex with OUL252 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7PWM
- Type
- protein
- Length
- 393 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q460N3
- Ligands
- 8AQ
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 195 | — | Q460N3 |
| B | — | protein | 198 | — | Q460N3 |
Ligands and binding sites
- 8AQ · 4-(cyclohexylmethoxy)-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.
Compared structures
- 7PWM · PARP15 catalytic domain in complex with OUL252 · 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 7PWM · PDBe 7PWM · UniProt Q460N3
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