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Crystal structure of aminoglycoside acetyltransferase AAC(3)-iva, H154A mutant, in complex with gentamicin C1A
Analyse Crystal structure of aminoglycoside acetyltransferase AAC(3)-iva, H154A mutant… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6MN5
- Type
- protein
- Length
- 1,555 residues
- Chains
- 6
- 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
- LLL, ZN
- Pockets
- 15 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, E, F | Aminoglycoside N(3)-acetyltransferase, AAC(3)-iva (EC 2.3.1.81) | protein | 259 | 37% helix, 22% strand | Q306W4 |
| D | Aminoglycoside N(3)-acetyltransferase, AAC(3)-iva (EC 2.3.1.81) | protein | 260 | 37% helix, 21% strand | Q306W4 |
Ligands and binding sites
- LLL · (2R,3R,4R,5R)-2-((1S,2S,3R,4S,6R)-4,6-diamino-3-((2R, 3R,6S)-3-amino-6-(aminomethyl)-tetrahydro-2H-pyran-2-yloxy)-2-hydroxycyclohexyloxy)-5-methyl-4-(methylamino)-tetrahydro-2H-pyran-3,5-diol · ligand · 6 copies · chains A, B, C, D, E, F
- ZN · Zinc ion · metal · 6 copies · chains A, B, C, D, E, F
- EDO · 1,2-ethanediol · additive · 41 copies · chains A, B, C, F, D, E
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 12 copies · chains A, B, C, F, D, E
- GOL · Glycerol · additive · 5 copies · chains A, B, C, F, D
- PE3 · 3,6,9,12,15,18,21,24,27,30,33,36,39-tridecaoxahentetracontane-1,41-diol · additive · 3 copies · chains B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 618 | 0.69 | 0.78 | 74 | LLL, EPE, EDO |
| 2 | 685 | 0.68 | 0.77 | 82 | LLL, EPE, GOL, EDO |
| 3 | 753 | 0.68 | 0.75 | 82 | LLL, EPE, EDO |
| 4 | 358 | 0.63 | 0.79 | 36 | LLL, EDO |
| 5 | 293 | 0.62 | 0.79 | 34 | LLL |
Interfaces
6 interfaces between chains.
- A–D · 818 Ų buried · 11 hydrogen bonds · protein-protein
- B–C · 800 Ų buried · 12 hydrogen bonds · protein-protein
- D–E · 614 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 609 Ų buried · 10 hydrogen bonds · protein-protein
- C–F · 597 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 6MN5 · Crystal structure of aminoglycoside acetyltransferase AAC(3)-IVa, H154A mutant, in… · 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 6MN5 · PDBe 6MN5 · UniProt Q306W4
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