Research workbench
Pde-ubi-adpr
Analyse Pde-ubi-adpr in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ZQ4
- Type
- protein
- Length
- 843 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q6RCR1, P0CG48
- Ligands
- AMP
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, A | — | protein | 348 | — | Q6RCR1 |
| C | — | protein | 73 | — | P0CG48 |
| D | — | protein | 74 | — | P0CG48 |
Ligands and binding sites
- AMP · Adenosine monophosphate · ligand · 2 copies · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5ZQ4 · PDE-Ubi-ADPr · the same entry in another collection · chain B against B, 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 Q6RCR1
- Every structure of UniProt P0CG48
- Elsewhere: RCSB PDB 5ZQ4 · PDBe 5ZQ4 · UniProt Q6RCR1 · UniProt P0CG48
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