Research workbench
Crystal structure of phosphinothricin acetyltransferase from agrobacterium tumefaciens
Analyse Crystal structure of phosphinothricin acetyltransferase from agrobacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1YR0
- Type
- protein
- Length
- 652 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphinothricin acetyltransferase
- EC
- 2.3.1.-
- UniProt
- Q8UGX8
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Phosphinothricin acetyltransferase (EC 2.3.1.-) | protein | 163 | 35% helix, 36% strand | Q8UGX8 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 5 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1037 | 0.80 | 0.81 | 106 | SO4 |
| 2 | 1153 | 0.79 | 0.80 | 113 | SO4 |
| 3 | 316 | 0.64 | 0.81 | 49 | empty |
Interfaces
5 interfaces between chains.
- A–B · 1424 Ų buried · 22 hydrogen bonds · protein-protein
- C–D · 1414 Ų buried · 18 hydrogen bonds · protein-protein
- A–C · 573 Ų buried · 9 hydrogen bonds · protein-protein
- A–D · 72 Ų buried · 1 hydrogen bond · protein-protein
- B–C · 66 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 12 modified (engineered).
Compared structures
- 1YR0 · Crystal structure of phosphinothricin acetyltransferase from agrobacterium tumefaciens · 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 Q8UGX8
- Elsewhere: RCSB PDB 1YR0 · PDBe 1YR0 · UniProt Q8UGX8
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