Protein profile

PA5199

protein AmgS

Genome: NC_002516.2

Gene: amgS PA5199 Structure source: AlphaFold UniProt Q9HTZ0
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Amino acids 439
Annotations 8
Features 42
PDB binders 4
Druggability 0.724

Overview

Basic information about this protein and its source genome.

Accession
PA5199
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
amgS PA5199
Status
annotated
Amino acids
439
Structure source
AlphaFold
EC
2.7.13.3
GO
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:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. 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).

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 0.724
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

MKTPLWFPQSFFARTLWLVLIVVLFSKALTLVYLLMNEDVIVDRQYSHGAALTIRAFWAADEESRAAIAKASGLRWVPSSADQPGEQHWPYTEIFQRQMQMELGPDTETRLRIHQPSQLWVRAPSLGEGWLAVPLYPHPLRGQRIWSVLGWFLGIGLLSTAAAWIFVRQLSQPLKRLVVAARQFGQGRSVRLPLGPETPSEMAEVYRAFNQMAEDIEQGGRERELMLAGVSHDLRTPLTRLRLSLELLPESEREMVEDMIRDIEDMDAILDQFLAFIRDGRDEPVEEGDLTDLVREVVAPFNQTREQVRMALQPVPAMPLRRVSMKRLLGNLIDNALNHGGGSVEVASYVAGESAAPYVVLSVLDRGQGIDPAEVDSIFNPFIRGDKARGGKGTGLGLAIVKRIAAQHGGSVELRNRDGGGLEARVCLPLGLLLPRGAA

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

7
  • 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:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
  • 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.

42 records
Show feature table
Start End DB Term Name
284 431 SUPERFAMILY SSF55874 ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
284 431 InterPro IPR036890 Histidine kinase/HSP90-like ATPase superfamily
15 37 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
222 282 SMART SM00388 HisKA_10
222 282 InterPro IPR003661 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
166 218 Pfam PF00672 HAMP domain
166 218 InterPro IPR003660 HAMP domain
325 427 CDD cd16950 HATPase_EnvZ-like
145 167 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
168 439 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
168 221 ProSiteProfiles PS50885 HAMP domain profile.
168 221 InterPro IPR003660 HAMP domain
221 278 CDD cd00082 HisKA
221 278 InterPro IPR003661 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
37 144 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
165 277 Gene3D G3DSA:1.10.287.130 -
229 432 ProSiteProfiles PS50109 Histidine kinase domain profile.
229 432 InterPro IPR005467 Histidine kinase domain
12 36 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
320 432 SMART SM00387 HKATPase_4
320 432 InterPro IPR003594 Histidine kinase/HSP90-like ATPase
145 167 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
284 432 Gene3D G3DSA:3.30.565.10 -
284 432 InterPro IPR036890 Histidine kinase/HSP90-like ATPase superfamily
1 11 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
206 279 SUPERFAMILY SSF47384 Homodimeric domain of signal transducing histidine kinase
206 279 InterPro IPR036097 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain superfamily
168 221 SMART SM00304 HAMP_11
392 410 PRINTS PR00344 Bacterial sensor protein C-terminal signature
392 410 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
416 429 PRINTS PR00344 Bacterial sensor protein C-terminal signature
416 429 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
359 373 PRINTS PR00344 Bacterial sensor protein C-terminal signature
359 373 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
377 387 PRINTS PR00344 Bacterial sensor protein C-terminal signature
377 387 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
171 216 CDD cd06225 HAMP
325 430 Pfam PF02518 Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
325 430 InterPro IPR003594 Histidine kinase/HSP90-like ATPase
64 429 PANTHER PTHR44936 SENSOR PROTEIN CREC
224 278 Pfam PF00512 His Kinase A (phospho-acceptor) domain
224 278 InterPro IPR003661 Signal transduction histidine kinase, dimerisation/phosphoacceptor 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

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

Entry Method Resolution Chain Coverage Links Status
AlphaFold PA5199
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
2 0.705
4 0.458
20 0.239

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.

54 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)…
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
PG0
5UKV
P71815 120.1 Da LogP -0.36 TPSA 38.7 ✓ Ro5 ✓ Clean COCCOCCO

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.