MolNFT v1 · #14763 · protein
Structure of the mt-adprase in complex with adpr, a nudix enzyme
1MK1 · Adpr pyrophosphatase: “Structure of the mt-adprase in complex with adpr, a nudix enzyme”. X-ray diffraction, 1 ligand (APR), 2 pockets (best druggability 0.51). MolNFT v1 #14763 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 1MK1
- Type
- protein
- Length
- 187 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adpr pyrophosphatase
- EC
- 3.6.1.13
- UniProt
- O33199
- Ligands
- APR
- Pockets
- 2 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 22% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adpr pyrophosphatase (EC 3.6.1.13) | protein | 187 | 22% helix, 42% strand | O33199 |
Ligands and binding sites
- APR · Adenosine-5-diphosphoribose · ligand · 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 | 236 | 0.51 | 0.75 | 28 | APR |
| 2 | 71 | 0.35 | 0.76 | 20 | empty |
Compared structures
- 1MK1 · Structure of the MT-ADPRase in complex with ADPR, a Nudix enzyme · 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 O33199
- Elsewhere: RCSB PDB 1MK1 · PDBe 1MK1 · UniProt O33199
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.