Research workbench
Crystal structure of mouse ADP-ribosylhydrolase 3 (MARH3)
Analyse Crystal structure of mouse ADP-ribosylhydrolase 3 (MARH3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2QTY
- Type
- protein
- Length
- 674 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- POLY(ADP-ribose) glycohydrolase ARH3
- EC
- 3.2.1.143
- UniProt
- Q8CG72
- Ligands
- MG
- Pockets
- 3 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 67% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | POLY(ADP-ribose) glycohydrolase ARH3 (EC 3.2.1.143) | protein | 337 | 67% helix, 1% strand | Q8CG72 |
Ligands and binding sites
- MG · Magnesium ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 670 | 0.70 | 0.78 | 76 | empty |
| 2 | 103 | 0.51 | 0.82 | 29 | empty |
| 3 | 110 | 0.48 | 0.80 | 26 | empty |
Interfaces
1 interface between chains.
- A–B · 500 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
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 Q8CG72
- Elsewhere: RCSB PDB 2QTY · PDBe 2QTY · UniProt Q8CG72
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