Research workbench
Human ARTD8 (PARP14, BAL2) - catalytic domain in complex with A16(E)
Analyse Human ARTD8 (PARP14, BAL2) - catalytic domain in complex with A16(E) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4F1Q
- Type
- protein
- Length
- 362 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q460N5
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 183 | — | Q460N5 |
| B | — | protein | 179 | — | Q460N5 |
Compared structures
- 4F1Q · Human Artd8 (Parp14, Bal2) - catalytic domain in complex with A16(E) · 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 4F1Q · PDBe 4F1Q · UniProt Q460N5
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