Research workbench
Human [protein ADP-ribosylargenine] hydrolase ARH1 in complex with ADP-hpm
Analyse Human [protein ADP-ribosylargenine] hydrolase ARH1 in complex with ADP-hpm in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6G2A
- Type
- protein
- Length
- 361 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
- A3R, MG, CL
- Pockets
- 2 · best druggability 0.44
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 | 361 | 66% helix, 1% strand | P54922 |
Ligands and binding sites
- A3R · Adenosine Diphosphate (Hydroxymethyl)pyrrolidine monoalcohol · ligand · chains A
- MG · Magnesium ion · metal · 2 copies · chains A
- CL · Chloride ion · ion · chains A
- ACT · Acetate ion · additive · 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 101 | 0.44 | 0.79 | 31 | A3R |
| 2 | 56 | 0.28 | 0.74 | 14 | A3R |
Compared structures
- 6G2A · Human [protein ADP-ribosylargenine] hydrolase ARH1 in complex with ADP-HPM · 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 0.98
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 6G2A · PDBe 6G2A · UniProt P54922
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