MolNFT v1 · #23495 · protein
Structure and function of phenazine-biosynthesis protein phzf from pseudomonas fluorescens 2-79
1U1X · Phenazine biosynthesis protein phzf: “Structure and function of phenazine-biosynthesis protein phzf from pseudomonas fluorescens 2-79”. X-ray diffraction, 1 ligand (HHA), 1 pocket (best druggability 0.76). MolNFT v1 #23495 on…
- PDB
- 1U1X
- Type
- protein
- Length
- 557 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phenazine biosynthesis protein phzf
- UniProt
- Q51792
- Ligands
- HHA
- Pockets
- 1 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 21% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phenazine biosynthesis protein phzf | protein | 278 | 21% helix, 43% strand | Q51792 |
| B | Phenazine biosynthesis protein phzf | protein | 279 | 21% helix, 42% strand | Q51792 |
Ligands and binding sites
- HHA · (2S,3S)-trans-2,3-dihydro-3-hydroxyanthranilic acid · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 839 | 0.76 | 0.80 | 63 | empty |
Interfaces
1 interface between chains.
- A–B · 1465 Ų buried · 24 hydrogen bonds · protein-protein
Compared structures
- 1U1X · Structure and function of phenazine-biosynthesis protein PhzF from Pseudomonas… · the same entry in another collection · chain A against A, TM-score 1.00
- Q51792 · AlphaFold monomer V2.0 prediction for trans-2,3-dihydro-3-hydroxyanthranilate isomerase… · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q51792
- Elsewhere: RCSB PDB 1U1X · PDBe 1U1X · UniProt Q51792
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