Research workbench
Crystal structure of aminoglycoside acetyltransferase AAC(3)-xa
Analyse Crystal structure of aminoglycoside acetyltransferase AAC(3)-xa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7LAP
- Type
- protein
- Length
- 571 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aminoglycoside N(3)-acetyltransferase
- EC
- 2.3.1.81
- UniProt
- Q54216
- Ligands
- CL
- Pockets
- 4 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aminoglycoside N(3)-acetyltransferase (EC 2.3.1.81) | protein | 285 | 40% helix, 20% strand | Q54216 |
| B | Aminoglycoside N(3)-acetyltransferase (EC 2.3.1.81) | protein | 286 | 40% helix, 20% strand | Q54216 |
Ligands and binding sites
- CL · Chloride ion · ion · chains B
- FMT · Formic acid · additive · 9 copies · chains A, B
- TAR · D(-)-tartaric acid · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 643 | 0.76 | 0.82 | 90 | empty |
| 2 | 365 | 0.64 | 0.79 | 55 | empty |
| 3 | 101 | 0.44 | 0.79 | 22 | empty |
| 4 | 91 | 0.42 | 0.79 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 1624 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 7LAP · Crystal structure of aminoglycoside acetyltransferase AAC(3)-Xa · 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 Q54216
- Elsewhere: RCSB PDB 7LAP · PDBe 7LAP · UniProt Q54216
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