Research workbench
Crystal structure of the E. COLI histidine kinase narx sensor domain in complex with nitrate
Analyse Crystal structure of the E. COLI histidine kinase narx sensor domain in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3EZH
- Type
- protein
- Length
- 227 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NITRATE/NITRITE sensor protein narx
- EC
- 2.7.13.3
- UniProt
- P0AFA2
- Ligands
- NO3
- Pockets
- 2 · best druggability 0.33
Structure
x-ray diffraction · 2 distinct chains · 85% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NITRATE/NITRITE sensor protein narx (EC 2.7.13.3) | protein | 114 | 83% helix, 0% strand | P0AFA2 |
| B | NITRATE/NITRITE sensor protein narx (EC 2.7.13.3) | protein | 113 | 86% helix, 0% strand | P0AFA2 |
Ligands and binding sites
- NO3 · Nitrate ion · ion · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 65 | 0.33 | 0.76 | 18 | empty |
| 2 | 58 | 0.27 | 0.73 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 1024 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 3EZH · Crystal Structure of the E. coli Histidine Kinase NarX Sensor Domain in Complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- P0AFA2 · AlphaFold monomer V2.0 prediction for NITRATE/NITRITE sensor protein narx (P0AFA2) · a predicted model of the same protein · chain B 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 P0AFA2
- Elsewhere: RCSB PDB 3EZH · PDBe 3EZH · UniProt P0AFA2
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