MolNFT v1 · #119300 · protein
Crystal structure of the phenol-responsive sensory domain of the transcription activator poxr in complex with 4-nitrophenol
5FRX · Positive phenol-degradative gene regulator: “Crystal structure of the phenol-responsive sensory domain of the transcription activator poxr in complex with…”. X-ray diffraction, 2 ligands (NPO, ZN), 5 pockets (best druggability…
- PDB
- 5FRX
- Type
- protein
- Length
- 392 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Positive phenol-degradative gene regulator
- UniProt
- O84957
- Ligands
- NPO, ZN
- Pockets
- 5 · best druggability 0.44
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Positive phenol-degradative gene regulator | protein | 196 | 47% helix, 24% strand | O84957 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 64 | 0.44 | 0.83 | 14 | empty |
| 2 | 73 | 0.43 | 0.81 | 14 | empty |
| 3 | 61 | 0.41 | 0.81 | 18 | empty |
| 4 | 70 | 0.32 | 0.75 | 14 | empty |
| 5 | 50 | 0.25 | 0.73 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 2317 Ų buried · 41 hydrogen bonds · protein-protein
Compared structures
- 5FRX · crystal structure of the phenol-responsive sensory domain of the transcription activator… · 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 O84957
- Elsewhere: RCSB PDB 5FRX · PDBe 5FRX · UniProt O84957
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