Research workbench
Crystal structure of streptomyces hygroscopicus bialaphos resistance (bar) protein in complex with acetyl coenzyme a
Analyse Crystal structure of streptomyces hygroscopicus bialaphos resistance (bar)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5T7D
- Type
- protein
- Length
- 694 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphinothricin N-acetyltransferase
- EC
- 2.3.1.183
- UniProt
- P16426
- Ligands
- ACO
- Pockets
- 8 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Phosphinothricin N-acetyltransferase (EC 2.3.1.183) | protein | 173 | 34% helix, 34% strand | P16426 |
| C, D | Phosphinothricin N-acetyltransferase (EC 2.3.1.183) | protein | 174 | 34% helix, 33% strand | P16426 |
Ligands and binding sites
- ACO · Acetyl coenzyme *A · ligand · 4 copies · chains A, B, C, D
- ACT · Acetate ion · additive · 8 copies · chains A, B, D, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1079 | 0.82 | 0.83 | 116 | ACO, ACT |
| 2 | 442 | 0.76 | 0.84 | 57 | ACT, ACO |
| 3 | 96 | 0.72 | 0.95 | 25 | empty |
| 4 | 397 | 0.66 | 0.79 | 45 | ACO |
| 5 | 70 | 0.34 | 0.76 | 17 | empty |
Interfaces
5 interfaces between chains.
- B–D · 1557 Ų buried · 15 hydrogen bonds · protein-protein
- C–D · 490 Ų buried · 3 hydrogen bonds · protein-protein
- A–C · 323 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 314 Ų buried · 1 hydrogen bond · protein-protein
- A–D · 27 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- P16426 · AlphaFold monomer V2.0 prediction for phosphinothricin N-acetyltransferase (P16426) · a predicted model of the same protein · chain C against A, TM-score 0.99
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 P16426
- Elsewhere: RCSB PDB 5T7D · PDBe 5T7D · UniProt P16426
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