Research workbench
Aminoglycoside N-acetyltransferase AAC(6')-iy in complex with CoA and N-terminal HIS(6)-tag (crystal form 1)
Analyse Aminoglycoside N-acetyltransferase AAC(6')-iy in complex with CoA and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1S5K
- Type
- protein
- Length
- 287 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aminoglycoside 6'-N-acetyltransferase
- EC
- 2.3.1.82
- UniProt
- Q9R381
- Ligands
- COA, SO4
- Pockets
- 2 · best druggability 0.66
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aminoglycoside 6'-N-acetyltransferase (EC 2.3.1.82) | protein | 153 | 35% helix, 33% strand | Q9R381 |
| B | Aminoglycoside 6'-N-acetyltransferase (EC 2.3.1.82) | protein | 134 | 32% helix, 37% strand | Q9R381 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 583 | 0.66 | 0.76 | 60 | SO4, COA |
| 2 | 483 | 0.63 | 0.76 | 55 | SO4, COA |
Interfaces
1 interface between chains.
- A–B · 2081 Ų buried · 47 hydrogen bonds · protein-protein
Compared structures
- 1S5K · Aminoglycoside N-Acetyltransferase AAC(6')-Iy in Complex with CoA and N-terminal… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9R381 · AlphaFold monomer V2.0 prediction for aminoglycoside N(6')-acetyltransferase type 1… · a predicted model of the same protein · chain B against A, TM-score 0.95
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 Q9R381
- Elsewhere: RCSB PDB 1S5K · PDBe 1S5K · UniProt Q9R381
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