Research workbench
Crystal structure of phosphinothricin N-acetyltransferase from brucella ovis
Analyse Crystal structure of phosphinothricin N-acetyltransferase from brucella ovis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5DWM
- Type
- protein
- Length
- 717 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphinothricin N-acetyltransferase
- EC
- 2.3.1.-
- UniProt
- A0A0H3AQB6
- Pockets
- 4 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphinothricin N-acetyltransferase (EC 2.3.1.-) | protein | 180 | 34% helix, 32% strand | A0A0H3AQB6 |
| B, C, D | Phosphinothricin N-acetyltransferase (EC 2.3.1.-) | protein | 179 | 34% helix, 32% strand | A0A0H3AQB6 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 4 copies · chains A, B, C, D
- IMD · Imidazole · additive · 4 copies · chains B, C, D
- GOL · Glycerol · additive · chains D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 645 | 0.77 | 0.83 | 78 | empty |
| 2 | 376 | 0.75 | 0.85 | 49 | GOL |
| 3 | 416 | 0.75 | 0.84 | 51 | empty |
| 4 | 396 | 0.73 | 0.84 | 49 | empty |
Interfaces
5 interfaces between chains.
- C–D · 1735 Ų buried · 27 hydrogen bonds · protein-protein
- A–B · 1720 Ų buried · 25 hydrogen bonds · protein-protein
- B–C · 285 Ų buried · 0 hydrogen bonds · protein-protein
- A–C · 52 Ų buried · 0 hydrogen bonds · protein-protein
- B–D · 17 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 5DWM · Crystal structure of Phosphinothricin N-acetyltransferase from Brucella ovis · 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 A0A0H3AQB6
- Elsewhere: RCSB PDB 5DWM · PDBe 5DWM · UniProt A0A0H3AQB6
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