MolNFT v1 · #149495 · protein
Human [protein ADP-ribosylargenine] hydrolase ARH1 in complex with ADP-ribose
6G28 · [protein ADP-ribosylarginine] hydrolase: “Human [protein ADP-ribosylargenine] hydrolase ARH1 in complex with ADP-ribose”. X-ray diffraction, 3 ligands (AR6, MG, CL), 2 pockets (best druggability 0.55). MolNFT v1 #149495 on…
- PDB
- 6G28
- Type
- protein
- Length
- 359 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- [protein ADP-ribosylarginine] hydrolase
- EC
- 3.2.2.19
- UniProt
- P54922
- Ligands
- AR6, MG, CL
- Pockets
- 2 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 66% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | [protein ADP-ribosylarginine] hydrolase (EC 3.2.2.19) | protein | 359 | 66% helix, 1% strand | P54922 |
Ligands and binding sites
- AR6 · [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxy-oxolan-2-yl]methyl [hydroxy-[[(2R,3S,4R,5S)-3,4,5-trihydroxyoxolan-2-yl]methoxy]phosphoryl] hydrogen phosphate · ligand · chains A
- MG · Magnesium ion · metal · 2 copies · chains A
- CL · Chloride ion · ion · 3 copies · chains A
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 | 187 | 0.55 | 0.80 | 33 | AR6, MG |
| 2 | 54 | 0.32 | 0.77 | 13 | AR6 |
Compared structures
- 6G28 · Human [protein ADP-ribosylargenine] hydrolase ARH1 in complex with ADP-ribose · the same entry in another collection · chain A against A, TM-score 1.00
- P54922 · AlphaFold monomer V2.0 prediction for [protein ADP-ribosylarginine] hydrolase (P54922) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P54922
- Elsewhere: RCSB PDB 6G28 · PDBe 6G28 · UniProt P54922
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