Protein profile

PA4117

phytochrome BphP

Genome: NC_002516.2

Gene: PA4117 bphP Structure source: Experimental + AlphaFold UniProt Q9HWR3
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Amino acids 728
Annotations 12
Features 48
PDB binders 8
Druggability 0.815

Overview

Basic information about this protein and its source genome.

Accession
PA4117
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA4117 bphP
Status
annotated
Amino acids
728
Structure source
Experimental + AlphaFold
EC
2.7.13.3
GO
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0042802 Binding to an identical protein or proteins. GO:0000156 Responds to a phosphorelay sensor to initiate a change in cell state or activity. The activity of the response regulator is regulated by transfer of a phosphate from a histidine residue in the sensor, to an aspartate residue in the response regulator. Many but not all response regulators act as transcriptional regulators to elicit a response. 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:0009881 The function of absorbing and responding to incidental electromagnetic radiation, particularly visible light. The response may involve a change in conformation. GO:0030295 Binds to and increases the activity of a protein kinase, an enzyme which phosphorylates a protein.

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.

FPocket 0.815
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 11 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

11
  • GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
  • GO:0042802 Binding to an identical protein or proteins.
  • GO:0000156 Responds to a phosphorelay sensor to initiate a change in cell state or activity. The activity of the response regulator is regulated by transfer of a phosphate from a histidine residue in the sensor, to an aspartate residue in the response regulator. Many but not all response regulators act as transcriptional regulators to elicit a response.
  • 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:0009881 The function of absorbing and responding to incidental electromagnetic radiation, particularly visible light. The response may involve a change in conformation.
  • GO:0030295 Binds to and increases the activity of a protein kinase, an enzyme which phosphorylates a protein.
  • GO:0009584 The series of events in which a visible light stimulus is received by a cell and converted into a molecular signal. A visible light stimulus is electromagnetic radiation that can be perceived visually by an organism; for organisms lacking a visual system, this can be defined as light with a wavelength within the range 380 to 780 nm.
  • GO:0007234 The series of molecular signals generated in response to osmotic change, as mediated through a phosphorelay system. In S.cerevisiae, the osmosensor is the histidine kinase Sln1.
  • 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:0005515 Binding to a protein.

Sequence Features

Domain/signature hits from InterPro and related databases.

48 records
Show feature table
Start End DB Term Name
12 469 Gene3D G3DSA:3.30.450.40 -
12 469 InterPro IPR029016 GAF-like domain superfamily
510 721 ProSiteProfiles PS50109 Histidine kinase domain profile.
510 721 InterPro IPR005467 Histidine kinase domain
503 566 Pfam PF00512 His Kinase A (phospho-acceptor) domain
503 566 InterPro IPR003661 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
141 289 Pfam PF01590 GAF domain
141 289 InterPro IPR003018 GAF domain
494 567 Gene3D G3DSA:1.10.287.130 -
6 115 SUPERFAMILY SSF55785 PYP-like sensor domain (PAS domain)
6 115 InterPro IPR035965 PAS domain superfamily
139 313 SMART SM00065 gaf_1
139 313 InterPro IPR003018 GAF domain
494 566 SUPERFAMILY SSF47384 Homodimeric domain of signal transducing histidine kinase
494 566 InterPro IPR036097 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain superfamily
311 493 SUPERFAMILY SSF55781 GAF domain-like
611 716 Pfam PF02518 Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
611 716 InterPro IPR003594 Histidine kinase/HSP90-like ATPase
139 297 ProSiteProfiles PS50046 Phytochrome chromophore attachment site domain profile.
139 297 InterPro IPR016132 Phytochrome chromophore attachment domain
556 721 SUPERFAMILY SSF55874 ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
556 721 InterPro IPR036890 Histidine kinase/HSP90-like ATPase superfamily
501 562 CDD cd00082 HisKA
501 562 InterPro IPR003661 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
12 76 Pfam PF08446 PAS fold
12 76 InterPro IPR013654 PAS fold-2
503 566 SMART SM00388 HisKA_10
610 721 SMART SM00387 HKATPase_4
610 721 InterPro IPR003594 Histidine kinase/HSP90-like ATPase
324 496 Pfam PF00360 Phytochrome region
324 496 InterPro IPR013515 Phytochrome, central region
16 244 Gene3D G3DSA:3.30.450.20 PAS domain
456 474 PRINTS PR01033 Phytochrome signature
456 474 InterPro IPR001294 Phytochrome
241 262 PRINTS PR01033 Phytochrome signature
241 262 InterPro IPR001294 Phytochrome
339 359 PRINTS PR01033 Phytochrome signature
339 359 InterPro IPR001294 Phytochrome
422 441 PRINTS PR01033 Phytochrome signature
422 441 InterPro IPR001294 Phytochrome
154 173 PRINTS PR01033 Phytochrome signature
154 173 InterPro IPR001294 Phytochrome
60 721 PANTHER PTHR42878 TWO-COMPONENT HISTIDINE KINASE
313 487 Gene3D G3DSA:3.30.450.270 -
313 487 InterPro IPR043150 Phytochrome, PHY domain superfamily
128 307 SUPERFAMILY SSF55781 GAF domain-like
569 726 Gene3D G3DSA:3.30.565.10 -
569 726 InterPro IPR036890 Histidine kinase/HSP90-like ATPase superfamily

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

7 + 1

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

Entry Method Resolution Chain Coverage Links Status
PDB 3NHQ
X-ray 2.55 Å A,B,C,D,E,F,G,H
68.3% 1-497
PDBe RCSB PDBj File
Viewing
PDB 3NOT
X-ray 2.70 Å C
68.3% 1-497
PDBe RCSB PDBj File
Loaded
PDB 3NOP
X-ray 2.80 Å C
68.3% 1-497
PDBe RCSB PDBj File
Loaded
PDB 3G6O
X-ray 2.85 Å A,B
68.3% 1-497
PDBe RCSB PDBj File
Loaded
PDB 3C2W
X-ray 2.90 Å A,B,C,D,E,F,G,H
68.3% 1-497
PDBe RCSB PDBj File
Loaded
PDB 3IBR
X-ray 2.97 Å A,B
68.3% 1-497
PDBe RCSB PDBj File
Loaded
PDB 3NOU
X-ray 3.00 Å C
68.3% 1-497
PDBe RCSB PDBj File
Loaded
AlphaFold PA4117
AlphaFold — — full sequence — Loaded
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 0.815

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK Sticks Spheres Surfaces Score Probability Labels Zoom Positions
1 33.85 0.948
2 5.44 0.258
3 3.75 0.144
4 2.5 0.07
5 2.21 0.053

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.

58 records

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.

Show only:
Ligand Source crystal MW · LogP · TPSA Lipinski PAINS SMILES
BLA
3NHQ 2.55 Å Open crystal
582.7 Da LogP 4.81 TPSA 160.9 1 viol. ✓ Clean Cc1c(c([nH]c1\C=C/2\C(=C(C(=O)N2)C=C)C)\C=C/3\C…

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.