Research workbench
Crystal structure of aminoglycoside resistance enzyme ApmA, complex with paromomycin and coenzyme A
Analyse Crystal structure of aminoglycoside resistance enzyme ApmA, complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7UUM
- Type
- protein
- Length
- 274 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.74
- Source
- Staphylococcus aureus
- Molecule
- Aminocyclitol acetyltransferase ApmA
- UniProt
- A0A1D0AST6
- Ligands
- COA, PAR
- Pockets
- 2 · best druggability 0.35
Structure
x-ray diffraction · resolution 2.74 · 1 distinct chain · 32% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aminocyclitol acetyltransferase ApmA | protein | 274 | 32% helix, 20% strand | A0A1D0AST6 |
Ligands and binding sites
- COA · Coenzyme A · ligand · chains A
- PAR · Paromomycin · ligand · chains A
- GOL · Glycerol · additive · 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 | 59 | 0.35 | 0.77 | 12 | empty |
| 2 | 58 | 0.35 | 0.78 | 15 | empty |
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 A0A1D0AST6
- Elsewhere: RCSB PDB 7UUM · PDBe 7UUM · UniProt A0A1D0AST6
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