Overview
Basic information about this protein and its source genome.
- Accession
- PA3878
- Gene
- GUL26_00735 PA3878 IPC1295_14005 narX PAERUG_P19_London_7_VIM_2_05_10_06654
- Status
- annotated
- Amino acids
- 622
- Structure source
- AlphaFold
Target profile
Computed evidence for target prioritization.
- Human off-target
- No hit
- Gut microbiome off-target
- hit
- Essential (DEG)
- N
- Localization
- CytoplasmicMembrane
Selected Druggability evidence
Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.
Sequence
Primary amino-acid sequence viewer.
MNKATAPDADQRDRFFGGSDRAGKPILRRSLVVRFGCYLTLLVSLALIGMFSALLFADYTHQDAAVINHAGSLRMLTYRVALEPSLEGRQALLGTLGERLDSGDIRRLLQRQDADDPIRQLHQELREGLARLDPRALPGRAVLDAYVGDIDRFVGILQAKAERRSQLLSTVQGLCLFLSLLVVFVTLYDLSYHVIGPLRELTSTARRLGRGELDARVTYSGEDELAQLGERFNQMAGELKSIYGDLEERVEDKTRALSQSHQRLELLYASARRLGENPYDSRTLQPLLNQLEKVLDAGRVTLCLNKDGVERAYSSLTTTERPADFCLQGDCGSCREQASACDQPSSLAQPLLMQPLSIAGHRFGELFIESRSGRLENWQQQLIETFCDNIARTFALSLQQEQESRLALFAERGTIARELHDSLAQSLSYLKIQVSRLGTLLKREAPAEKIEDTLDELREGLNGAYRQLRELLTTFRLSLDEPSLEAALGNAVAEFGERGEVTIELDNRLQHVPLSPNEEIHVLQIVREALSNVVRHSQAQRAWVRLSSQADGQVSIAVEDDGVGFDPQQNRSGHYGLTIMQERGQTLGSQLRFEARAPHGTRVLFSFVPTALQPSAAKEPTP
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Enzyme Commission (EC)
1Gene Ontology (GO)
8- GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
- GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
- GO:0000155 Catalysis of the phosphorylation of a histidine residue in response to detection of an extracellular signal such as a chemical ligand or change in environment, to initiate a change in cell state or activity. The two-component sensor is a histidine kinase that autophosphorylates a histidine residue in its active site. The phosphate is then transferred to an aspartate residue in a downstream response regulator, to trigger a response.
- GO:0046983 The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits.
- GO:0007165 The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell.
- GO:0000160 A conserved series of molecular signals found in prokaryotes and eukaryotes; involves autophosphorylation of a histidine kinase and the transfer of the phosphate group to an aspartate that then acts as a phospho-donor to response regulator proteins.
- GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
- GO:0004673 Catalysis of the reaction: ATP + protein L-histidine = ADP + protein phospho-L-histidine.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 522 | 603 | CDD | cd16917 | HATPase_UhpB-NarQ-NarX-like |
| 193 | 242 | SUPERFAMILY | SSF158472 | HAMP domain-like |
| 17 | 622 | PIRSF | PIRSF003167 | HK_NarX/NarQ |
| 17 | 622 | InterPro | IPR016380 | Signal transduction histidine kinase, nitrate/nitrite-sensing |
| 477 | 610 | Gene3D | G3DSA:3.30.565.10 | - |
| 477 | 610 | InterPro | IPR036890 | Histidine kinase/HSP90-like ATPase superfamily |
| 411 | 476 | Pfam | PF07730 | Histidine kinase |
| 411 | 476 | InterPro | IPR011712 | Signal transduction histidine kinase, subgroup 3, dimerisation and phosphoacceptor domain |
| 447 | 474 | Coils | Coil | Coil |
| 27 | 613 | PANTHER | PTHR24421 | NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED |
| 189 | 622 | Phobius | NON_CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. |
| 391 | 473 | Gene3D | G3DSA:1.20.5.1930 | - |
| 58 | 166 | Phobius | CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm. |
| 192 | 244 | SMART | SM00304 | HAMP_11 |
| 192 | 244 | InterPro | IPR003660 | HAMP domain |
| 62 | 101 | Pfam | PF13675 | Type IV pili methyl-accepting chemotaxis transducer N-term |
| 62 | 101 | InterPro | IPR029095 | NarX-like, N-terminal |
| 517 | 611 | SMART | SM00387 | HKATPase_4 |
| 517 | 611 | InterPro | IPR003594 | Histidine kinase/HSP90-like ATPase |
| 518 | 608 | Pfam | PF02518 | Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase |
| 518 | 608 | InterPro | IPR003594 | Histidine kinase/HSP90-like ATPase |
| 192 | 240 | Pfam | PF00672 | HAMP domain |
| 192 | 240 | InterPro | IPR003660 | HAMP domain |
| 414 | 611 | ProSiteProfiles | PS50109 | Histidine kinase domain profile. |
| 414 | 611 | InterPro | IPR005467 | Histidine kinase domain |
| 167 | 188 | Phobius | TRANSMEMBRANE | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 195 | 239 | CDD | cd06225 | HAMP |
| 31 | 57 | Phobius | TRANSMEMBRANE | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 161 | 251 | Gene3D | G3DSA:6.10.340.10 | - |
| 35 | 57 | TMHMM | TMhelix | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 1 | 30 | Phobius | NON_CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. |
| 173 | 195 | TMHMM | TMhelix | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 192 | 244 | ProSiteProfiles | PS50885 | HAMP domain profile. |
| 508 | 608 | SUPERFAMILY | SSF55874 | ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase |
| 508 | 608 | InterPro | IPR036890 | Histidine kinase/HSP90-like ATPase superfamily |
| 63 | 160 | Gene3D | G3DSA:1.20.120.960 | Histidine kinase NarX, sensor domain |
| 63 | 160 | InterPro | IPR042295 | NarX-like, N-terminal domain superfamily |
3D Structure
Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.
Loading 3D structure...
Structural evidence
0 + 1Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold
PA3878
|
AlphaFold | — | — | full sequence | — | Viewing |
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer
Pockets (FPOCKET)
Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).
| FPOCKET | Sticks | Spheres | Surfaces | Druggability | Labels | Zoom | Positions |
|---|---|---|---|---|---|---|---|
| 1 | 0.643 | ||||||
| 5 | 0.631 |
Ligand evidence
Ligands grouped by evidence source. PDB ligands keep the source crystal visible, and loaded crystals can be opened directly in the structure viewer.
Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, use Open crystal to inspect it in the structure viewer.
No PDB structure with a co-crystallized ligand found for this exact protein.
Structural evidence inferred from similar proteins. The source crystal indicates where the ligand was observed; the UniProt column identifies the homologous protein carrying that ligand.
| Ligand | Source crystal | UniProt (homolog) | MW · LogP · TPSA | Lipinski | PAINS | SMILES |
|---|---|---|---|---|---|---|
| LFA | P27896 | 282.6 Da LogP 8.05 TPSA 0.0 | 1 viol. | ✓ Clean |
CCCCCCCCCCCCCCCCCCCC
|
Experimental bioactivity from ChEMBL measured directly on this protein. Score = pchembl (−log Ki/IC₅₀; higher = more potent).
No ChEMBL bioactivity data found for this exact protein.
Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).
No ChEMBL hits found through similar proteins.
Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).
| Ligand | Tanimoto | MW · LogP · TPSA | Lipinski | PAINS | SMILES |
|---|---|---|---|---|---|
| ZINC1545440 | 0.615 | 213.4 Da LogP 4.65 TPSA 26.0 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCCCCN
|
| ZINC1644076 | 0.615 | 214.4 Da LogP 4.68 TPSA 20.2 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCCCCO
|
| ZINC1680803 | 0.615 | 200.4 Da LogP 4.29 TPSA 20.2 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCCCO
|
| ZINC195766643 | 0.615 | 231.9 Da LogP 2.93 TPSA 0.0 | ✓ Ro5 | ✓ Clean |
CCCCCCCC[Sn+3]
|
| ZINC59144932 | 0.615 | 202.4 Da LogP 4.84 TPSA 0.0 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCCS
|
| ZINC100027350 | 0.571 | 227.4 Da LogP 4.91 TPSA 12.0 | ✓ Ro5 | ✓ Clean |
CCCCCCCCNCCCCCCC
|
| ZINC1627284 | 0.571 | 214.4 Da LogP 4.94 TPSA 9.2 | ✓ Ro5 | ✓ Clean |
CCCCCCCOCCCCCCC
|
| ZINC1699899 | 0.571 | 202.4 Da LogP 4.88 TPSA 0.0 | ✓ Ro5 | ✓ Clean |
CCCCCCSCCCCCC
|
| ZINC1724011 | 0.571 | 213.4 Da LogP 4.52 TPSA 12.0 | ✓ Ro5 | ✓ Clean |
CCCCCCCNCCCCCCC
|
| ZINC2564179 | 0.571 | 214.4 Da LogP 4.94 TPSA 9.2 | ✓ Ro5 | ✓ Clean |
CCCCCCCCOCCCCCC
|
| ZINC100050955 | 0.533 | 327.6 Da LogP 4.48 TPSA 36.1 | ✓ Ro5 | ✓ Clean |
CCCCCCCCNCCNCCNCCCCCCCC
|
| ZINC100077022 | 0.533 | 227.4 Da LogP 4.86 TPSA 3.2 | ✓ Ro5 | ✓ Clean |
CCCCCCCN(C)CCCCCCC
|
| ZINC100924963 | 0.533 | 284.5 Da LogP 4.89 TPSA 24.1 | ✓ Ro5 | ✓ Clean |
CCCCCCCCNCCNCCCCCCCC
|
| ZINC106401282 | 0.533 | 227.4 Da LogP 4.91 TPSA 12.0 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCCCCNC
|
| ZINC1673414 | 0.533 | 228.4 Da LogP 4.61 TPSA 0.0 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCC[N+](C)(C)C
|
| ZINC1687260 | 0.533 | 213.4 Da LogP 4.47 TPSA 3.2 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCCN(C)C
|
| ZINC1700269 | 0.533 | 200.4 Da LogP 3.83 TPSA 0.0 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCC[N+](C)(C)C
|
| ZINC2555244 | 0.533 | 227.4 Da LogP 4.86 TPSA 3.2 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCCCN(C)C
|
| ZINC35052519 | 0.533 | 228.4 Da LogP 3.33 TPSA 24.1 | ✓ Ro5 | ✓ Clean |
CCCCCCNCCNCCCCCC
|
| ZINC59359855 | 0.533 | 231.5 Da LogP 4.79 TPSA 0.0 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCC[S+](C)C
|
| ZINC100015910 | 0.500 | 214.4 Da LogP 4.68 TPSA 20.2 | ✓ Ro5 | ✓ Clean |
CCCCCCC[C@@H](O)CCCCCC
|
| ZINC114881475 | 0.500 | 206.4 Da LogP 4.31 TPSA 0.0 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCC(S)S
|
| ZINC1593347 | 0.500 | 246.5 Da LogP 4.68 TPSA 17.1 | ✓ Ro5 | ✓ Clean |
CCCCCCCS(=O)CCCCCCC
|
| ZINC1599570 | 0.500 | 227.4 Da LogP 4.86 TPSA 3.2 | ✓ Ro5 | ✓ Clean |
CCCCCN(CCCCC)CCCCC
|
| ZINC1605994 | 0.500 | 202.4 Da LogP 4.88 TPSA 0.0 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCSCC
|
| ZINC1606032 | 0.500 | 200.4 Da LogP 4.29 TPSA 20.2 | ✓ Ro5 | ✓ Clean |
CCCCCCC[C@@H](O)CCCCC
|
| ZINC1606040 | 0.500 | 214.4 Da LogP 4.68 TPSA 20.2 | ✓ Ro5 | ✓ Clean |
CCCCCCCC[C@@H](O)CCCCC
|
| ZINC1606049 | 0.500 | 200.4 Da LogP 4.29 TPSA 20.2 | ✓ Ro5 | ✓ Clean |
CCCCCCC(O)CCCCCC
|
| ZINC1672455 | 0.500 | 226.4 Da LogP 4.07 TPSA 34.1 | ✓ Ro5 | Alert |
CCCCCCC(=O)C(=O)CCCCCC
|
| ZINC1687262 | 0.500 | 213.4 Da LogP 4.52 TPSA 12.0 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCCNCC
|
| ZINC1693894 | 0.500 | 212.4 Da LogP 4.89 TPSA 17.1 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCCCC=O
|
| ZINC1697133 | 0.500 | 214.4 Da LogP 4.94 TPSA 9.2 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCCOCC
|
| ZINC169808442 | 0.500 | 305.1 Da LogP 4.57 TPSA 17.1 | ✓ Ro5 | ✓ Clean |
CCCCCC[Sn](=O)CCCCCC
|
| ZINC196468891 | 0.500 | 261.0 Da LogP 3.91 TPSA 0.0 | ✓ Ro5 | ✓ Clean |
CCCCC[Sn+2]CCCCC
|
| ZINC20231719 | 0.500 | 234.4 Da LogP 3.56 TPSA 34.1 | ✓ Ro5 | ✓ Clean |
CCCCCCS(=O)(=O)CCCCCC
|
| ZINC2166283 | 0.500 | 262.5 Da LogP 4.34 TPSA 34.1 | ✓ Ro5 | ✓ Clean |
CCCCCCCCS(=O)(=O)CCCCCC
|
| ZINC221753674 | 0.500 | 324.3 Da LogP 4.61 TPSA 0.0 | ✓ Ro5 | ✓ Clean |
CCCCCCC[Sn](Cl)(Cl)Cl
|
| ZINC2508105 | 0.500 | 200.4 Da LogP 4.29 TPSA 20.2 | ✓ Ro5 | ✓ Clean |
CCCCCCC[C@H](O)CCCCC
|
| ZINC2509968 | 0.500 | 214.4 Da LogP 4.68 TPSA 20.2 | ✓ Ro5 | ✓ Clean |
CCCCCCC[C@H](O)CCCCCC
|
| ZINC2528299 | 0.500 | 214.4 Da LogP 4.68 TPSA 20.2 | ✓ Ro5 | ✓ Clean |
CCCCCCCC[C@H](O)CCCCC
|
| ZINC2900787 | 0.500 | 228.4 Da LogP 4.61 TPSA 0.0 | ✓ Ro5 | ✓ Clean |
CCCCCCCCC[N+](CC)(CC)CC
|
| ZINC45331803 | 0.500 | 201.4 Da LogP 3.80 TPSA 35.2 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCCON
|
| ZINC59631801 | 0.500 | 200.4 Da LogP 3.37 TPSA 38.0 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCCNN
|
| ZINC60107866 | 0.500 | 242.5 Da LogP 4.41 TPSA 24.1 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCCNNCCC
|
| ZINC71773056 | 0.500 | 200.4 Da LogP 3.32 TPSA 29.3 | ✓ Ro5 | ✓ Clean |
CCCCCCN(N)CCCCCC
|
| ZINC97973035 | 0.500 | 212.4 Da LogP 4.23 TPSA 49.9 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCCC(=N)N
|
PDB and ChEMBL records on this protein are shown in full. ChEMBL records from similar proteins are capped at the top 100 per protein (by pchembl) and ZINC at the top 50 (Tanimoto ≥ 0.5). ADME columns are descriptor-based screening flags, not experimental toxicity results.