Research workbench
ADP-ribosylserine hydrolase ARH3 of latimeria chalumnae in complex with ADP-ribose
Analyse ADP-ribosylserine hydrolase ARH3 of latimeria chalumnae in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6G1Q
- Type
- protein
- Length
- 661 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- H3BCW1
- Ligands
- AR6, MG
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 330 | — | H3BCW1 |
| B | — | protein | 331 | — | H3BCW1 |
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 · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6G1Q · ADP-ribosylserine hydrolase ARH3 of Latimeria chalumnae in complex with ADP-ribose · the same entry in another collection · chain A against A, TM-score 1.00
- H3BCW1 · AlphaFold monomer V2.0 prediction for ADP-ribose glycohydrolase ARH3 (H3BCW1) · 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 H3BCW1
- Elsewhere: RCSB PDB 6G1Q · PDBe 6G1Q · UniProt H3BCW1
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