MolNFT v1 · #72180 · protein
Crystal structure of BA2930 mutant (H183A) in complex with accoa
3N0S · Aminoglycoside N3-acetyltransferase: “Crystal structure of BA2930 mutant (H183A) in complex with accoa”. X-ray diffraction, 2 ligands (ACO, MG), 12 pockets (best druggability 0.81). MolNFT v1 #72180 on GenesisL1: 3D structure…
- PDB
- 3N0S
- Type
- protein
- Length
- 1,060 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aminoglycoside N3-acetyltransferase
- EC
- 2.3.1.81
- UniProt
- Q81P86
- Ligands
- ACO, MG
- Pockets
- 12 · best druggability 0.81
Structure
x-ray diffraction · 3 distinct chains · 40% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Aminoglycoside N3-acetyltransferase (EC 2.3.1.81) | protein | 265 | 40% helix, 22% strand | Q81P86 |
| C | Aminoglycoside N3-acetyltransferase (EC 2.3.1.81) | protein | 264 | 40% helix, 22% strand | Q81P86 |
| B | Aminoglycoside N3-acetyltransferase (EC 2.3.1.81) | protein | 266 | 39% helix, 22% strand | Q81P86 |
Ligands and binding sites
- ACO · Acetyl coenzyme *A · ligand · 4 copies · chains A, D, C, B
- MG · Magnesium ion · metal · 2 copies · chains D, B
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1006 | 0.81 | 0.83 | 99 | MG |
| 2 | 848 | 0.78 | 0.81 | 80 | empty |
| 3 | 829 | 0.77 | 0.81 | 69 | empty |
| 4 | 746 | 0.76 | 0.80 | 66 | empty |
| 5 | 542 | 0.70 | 0.79 | 40 | empty |
Interfaces
6 interfaces between chains.
- D–C · 1518 Ų buried · 4 hydrogen bonds · protein-protein
- A–B · 1485 Ų buried · 3 hydrogen bonds · protein-protein
- D–B · 425 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 262 Ų buried · 6 hydrogen bonds · protein-protein
- C–B · 168 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 36 modified (engineered).
Compared structures
- 3N0S · Crystal structure of BA2930 mutant (H183A) in complex with AcCoA · 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 Q81P86
- Elsewhere: RCSB PDB 3N0S · PDBe 3N0S · UniProt Q81P86
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