Research workbench
X-ray crystal structure of phzg from pseudomonas fluorescens
Analyse X-ray crystal structure of phzg from pseudomonas fluorescens in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TY9
- Type
- protein
- Length
- 409 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phenazine biosynthesis protein phzg
- UniProt
- Q51793
- Ligands
- FMN, SO4
- Pockets
- 4 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 28% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phenazine biosynthesis protein phzg | protein | 202 | 28% helix, 39% strand | Q51793 |
| B | Phenazine biosynthesis protein phzg | protein | 207 | 29% helix, 37% strand | Q51793 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 613 | 0.80 | 0.85 | 68 | FMN |
| 2 | 440 | 0.72 | 0.83 | 45 | FMN |
| 3 | 97 | 0.40 | 0.77 | 15 | empty |
| 4 | 89 | 0.34 | 0.75 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 2950 Ų buried · 56 hydrogen bonds · protein-protein
Compared structures
- 1TY9 · X-ray crystal structure of phzg from pseudomonas fluorescens · the same entry in another collection · chain A against A, TM-score 1.00
- Q51793 · AlphaFold monomer V2.0 prediction for dihydrophenazinedicarboxylate synthase (Q51793) · a predicted model of the same protein · chain A 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 Q51793
- Elsewhere: RCSB PDB 1TY9 · PDBe 1TY9 · UniProt Q51793
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