MolNFT v1 · #24869 · protein
Crystal structure analusis of the ADP-ribose pyrophosphatase complexed with AMP and mg
1V8S: “Crystal structure analusis of the ADP-ribose pyrophosphatase complexed with AMP and mg”. X-ray diffraction, 2 ligands (AMP, MG), 1 pocket (best druggability 0.50). MolNFT v1 #24869 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1V8S
- Type
- protein
- Length
- 152 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ADP-ribose pyrophosphatase
- EC
- 3.6.1.13
- UniProt
- Q84CU3
- Ligands
- AMP, MG
- Pockets
- 1 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 23% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ADP-ribose pyrophosphatase (EC 3.6.1.13) | protein | 152 | 23% helix, 45% strand | Q84CU3 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 200 | 0.50 | 0.76 | 29 | empty |
Compared structures
- 1V8S · Crystal structure analusis of the ADP-ribose pyrophosphatase complexed with AMP and Mg · the same entry in another collection · chain A against A, TM-score 1.00
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 Q84CU3
- Elsewhere: RCSB PDB 1V8S · PDBe 1V8S · UniProt Q84CU3
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