MolNFT v1 · #149497 · protein
Human [protein ADP-ribosylargenine] hydrolase ARH1 in complex with ADP-hpm
6G2A: “Human [protein ADP-ribosylargenine] hydrolase ARH1 in complex with ADP-hpm”. X-ray diffraction, 3 ligands (A3R, MG, CL). MolNFT v1 #149497 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6G2A
- Type
- protein
- Length
- 361 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P54922
- Ligands
- A3R, MG, CL
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 361 | — | 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.
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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