MolNFT v1 · #157056 · protein
Crystal structure of aminoglycoside acetyltransferase AAC(3)-iva, apoenzyme
6MN3 · Aminoglycoside N(3)-acetyltransferase, AAC(3)-iva: “Crystal structure of aminoglycoside acetyltransferase AAC(3)-iva, apoenzyme”. X-ray diffraction, 2 ligands (ZN, CL), 2 pockets (best druggability 0.59). MolNFT v1 #157056 on…
- PDB
- 6MN3
- Type
- protein
- Length
- 514 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aminoglycoside N(3)-acetyltransferase, AAC(3)-iva
- EC
- 2.3.1.81
- UniProt
- Q306W4
- Ligands
- ZN, CL
- Pockets
- 2 · best druggability 0.59
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aminoglycoside N(3)-acetyltransferase, AAC(3)-iva (EC 2.3.1.81) | protein | 255 | 37% helix, 20% strand | Q306W4 |
| B | Aminoglycoside N(3)-acetyltransferase, AAC(3)-iva (EC 2.3.1.81) | protein | 259 | 37% helix, 21% strand | Q306W4 |
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 | 287 | 0.59 | 0.78 | 33 | empty |
| 2 | 274 | 0.57 | 0.77 | 36 | empty |
Interfaces
1 interface between chains.
- A–B · 457 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 6MN3 · Crystal structure of aminoglycoside acetyltransferase AAC(3)-IVa, apoenzyme · 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 Q306W4
- Elsewhere: RCSB PDB 6MN3 · PDBe 6MN3 · UniProt Q306W4
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