Research workbench
Crystal structure of human PARP14 bound to 2-{[(1-methylpiperidin-4- YL)METHYL]AMINO}-5,6,7,8-TETRAHYDRO[1]BENZOTHIENO[2,3-D]PYRIMIDIN- 4(3H)-one inhibitor
Analyse Crystal structure of human PARP14 bound to 2-{[(1-methylpiperidin-4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5V7W
- Type
- protein
- Length
- 347 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Poly [ADP-ribose] polymerase 14
- EC
- 2.4.2.30
- UniProt
- Q460N5
- Ligands
- 91J
- Pockets
- 2 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 25% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Poly [ADP-ribose] polymerase 14 (EC 2.4.2.30) | protein | 169 | 27% helix, 37% strand | Q460N5 |
| B | Poly [ADP-ribose] polymerase 14 (EC 2.4.2.30) | protein | 178 | 24% helix, 35% strand | Q460N5 |
Ligands and binding sites
- 91J · 2-{[(1-methylpiperidin-4-yl)methyl]amino}-5,6,7,8-tetrahydro[1]benzothieno[2,3-d]pyrimidin-4(3H)-one · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 534 | 0.69 | 0.79 | 90 | 91J |
| 2 | 78 | 0.32 | 0.74 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 706 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 5V7W · Crystal structure of human PARP14 bound to 2-{[(1-methylpiperidin-4-yl)methyl]amino}-5,6,7… · 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 Q460N5
- Elsewhere: RCSB PDB 5V7W · PDBe 5V7W · UniProt Q460N5
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.