Protein profile

PA5124

two-component sensor NtrB

Genome: NC_002516.2

Gene: PA5124 ntrB Structure source: AlphaFold UniProt Q9HU60
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Amino acids 358
Annotations 9
Features 37
PDB binders 5
Druggability 0.752

Overview

Basic information about this protein and its source genome.

Accession
PA5124
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA5124 ntrB
Status
annotated
Amino acids
358
Structure source
AlphaFold
EC
2.7.13.3
GO
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. 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:0006355 Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription. 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.

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
Gut microbiome off-target
hit
Essential (DEG)
Y
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.

FPocket 0.752
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

MPTDTLHRLLLDNLTTAVILLNGELRLEYMNPAAEMLLAVSGQRSHGQFISELFTESPEALNSLRQAVEQAHPFTKREATLTSITGVSITVDYAVTPILNRNETLLLLEVHPRDRLMRITREEAQLSKQETTKLLVRGLAHEIKNPLGGIRGAAQLLSRELPEESLKDYTNVIIEEADRLRNLVDRMLGSNKLPNLAPTNIHEVLERVSSLVEAESQGSITLVRDYDPSIPDLLLDREQMIQAVLNMVRNAMQAIAGQNDLRLGRITLRSRTLRQFTIGHTRHRLVCKVEIIDNGPGIPAELQETIFYPMVSGRPDGTGLGLAIAQNIISQHQGLIECESHPGHTVFSLFLPLEQGVH

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

8
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
  • GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.
  • 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:0006355 Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription.
  • 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:0016772 Catalysis of the transfer of a phosphorus-containing group from one compound (donor) to another (acceptor).
  • GO:0016310 The process of introducing a phosphate group into a molecule, usually with the formation of a phosphoric ester, a phosphoric anhydride or a phosphoric amide.

Sequence Features

Domain/signature hits from InterPro and related databases.

37 records
Show feature table
Start End DB Term Name
5 73 SMART SM00091 pas_2
5 73 InterPro IPR000014 PAS domain
8 104 Pfam PF00989 PAS fold
8 104 InterPro IPR013767 PAS fold
339 352 PRINTS PR00344 Bacterial sensor protein C-terminal signature
339 352 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
316 334 PRINTS PR00344 Bacterial sensor protein C-terminal signature
316 334 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
287 301 PRINTS PR00344 Bacterial sensor protein C-terminal signature
287 301 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
236 355 Pfam PF02518 Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
236 355 InterPro IPR003594 Histidine kinase/HSP90-like ATPase
3 114 Gene3D G3DSA:3.30.450.20 PAS domain
5 355 PANTHER PTHR43065 SENSOR HISTIDINE KINASE
240 352 CDD cd16918 HATPase_Glnl-NtrB-like
194 355 FunFam G3DSA:3.30.565.10:FF:000008 Nitrogen regulation histidine kinase
135 188 Pfam PF00512 His Kinase A (phospho-acceptor) domain
135 188 InterPro IPR003661 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
125 193 SUPERFAMILY SSF47384 Homodimeric domain of signal transducing histidine kinase
125 193 InterPro IPR036097 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain superfamily
195 354 Gene3D G3DSA:3.30.565.10 -
195 354 InterPro IPR036890 Histidine kinase/HSP90-like ATPase superfamily
117 192 FunFam G3DSA:1.10.287.130:FF:000005 Nitrogen regulation histidine kinase
6 104 SUPERFAMILY SSF55785 PYP-like sensor domain (PAS domain)
6 104 InterPro IPR035965 PAS domain superfamily
198 353 SUPERFAMILY SSF55874 ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
198 353 InterPro IPR036890 Histidine kinase/HSP90-like ATPase superfamily
138 355 ProSiteProfiles PS50109 Histidine kinase domain profile.
138 355 InterPro IPR005467 Histidine kinase domain
135 188 CDD cd00082 HisKA
131 196 SMART SM00388 HisKA_10
131 196 InterPro IPR003661 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
116 192 Gene3D G3DSA:1.10.287.130 -
235 355 SMART SM00387 HKATPase_4
235 355 InterPro IPR003594 Histidine kinase/HSP90-like ATPase
14 114 CDD cd00130 PAS
14 114 InterPro IPR000014 PAS domain

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

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Structural evidence

0 + 1

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry Method Resolution Chain Coverage Links Status
AlphaFold PA5124
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
3 0.752

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.

55 records

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.

Show only:
Ligand Source crystal UniProt (homolog) MW · LogP · TPSA Lipinski PAINS SMILES
ANP
4BIW
P0AE82 506.2 Da LogP -2.06 TPSA 281.9 3 viol. ✓ Clean c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…
C2E
5IDM
Q9X688 690.4 Da LogP -3.05 TPSA 349.6 3 viol. ✓ Clean c1nc2c(n1[C@H]3[C@@H]([C@H]4[C@H](O3)CO[P@@](=O…
CMO
1XJ2
P23222 28.0 Da LogP -0.04 TPSA 19.9 ✓ Ro5 ✓ Clean [C-]#[O+]
EMC
3A0W
Q9X180 229.7 Da LogP 0.97 TPSA 0.0 ✓ Ro5 ✓ Clean CC[Hg+]
EMT
3A0W
Q9X180 382.8 Da LogP 2.91 TPSA 37.3 ✓ Ro5 ✓ Clean CC[Hg]Sc1ccccc1C(=O)O

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.