Research workbench
Human PARP14 (ARTD8), catalytic fragment in complex with inhibitor H5
Analyse Human PARP14 (ARTD8), catalytic fragment in complex with inhibitor H5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5LXP
- Type
- protein
- Length
- 363 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q460N5
- Ligands
- 7AG
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 182 | — | Q460N5 |
| B | — | protein | 181 | — | Q460N5 |
Ligands and binding sites
- 7AG · ~{N}'-(3-aminocarbonylphenyl)-~{N}-[[1-[(2~{R})-2-phenylpropyl]-1,2,3-triazol-4-yl]methyl]pentanediamide · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5LXP · Human PARP14 (ARTD8), catalytic fragment in complex with inhibitor H5 · the same entry in another collection · chain A against A, TM-score 1.00
- Q460N5 · AlphaFold monomer V2.0 prediction for protein mono-ADP- ribosyltransferase PARP14 (Q460N5) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 5LXP · PDBe 5LXP · UniProt Q460N5
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