Protein profile

PA1930

chemotaxis transducer

Genome: NC_002516.2

Gene: PA1930 Structure source: AlphaFold UniProt Q9I2H4

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Amino acids 431

Annotations 6

Features 47

PDB binders 2

Druggability 0.783

Overview

Basic information about this protein and its source genome.

Accession: PA1930
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA1930
Status: annotated
Amino acids: 431
Structure source: AlphaFold

GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. GO:0016301 Catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule. GO:0008276 Catalysis of the transfer of a methyl group (CH3-) to a protein. GO:0004888 Combining with an extracellular or intracellular signal and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity or state as part of signal transduction. GO:0006935 The directed movement of a motile cell or organism, or the directed growth of a cell guided by a specific chemical concentration gradient. Movement may be towards a higher concentration (positive chemotaxis) or towards a lower concentration (negative chemotaxis). 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): 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 0.783

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

6 GO

Gene Ontology (GO)

GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
GO:0016301 Catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule.
GO:0008276 Catalysis of the transfer of a methyl group (CH3-) to a protein.
GO:0004888 Combining with an extracellular or intracellular signal and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity or state as part of signal transduction.
GO:0006935 The directed movement of a motile cell or organism, or the directed growth of a cell guided by a specific chemical concentration gradient. Movement may be towards a higher concentration (positive chemotaxis) or towards a lower concentration (negative chemotaxis).
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.

Sequence Features

Domain/signature hits from InterPro and related databases.

47 records

Show feature table

Start	End	DB	Term	Name
91	143	ProSiteProfiles	PS50113	PAC domain profile.
91	143	InterPro	IPR000700	PAS-associated, C-terminal
30	132	SUPERFAMILY	SSF55785	PYP-like sensor domain (PAS domain)
30	132	InterPro	IPR035965	PAS domain superfamily
29	134	Pfam	PF08448	PAS fold
29	134	InterPro	IPR013656	PAS fold-4
38	62	ProSiteProfiles	PS50112	PAS repeat profile.
38	62	InterPro	IPR000014	PAS domain
248	428	SUPERFAMILY	SSF58104	Methyl-accepting chemotaxis protein (MCP) signaling domain
139	207	SMART	SM00091	pas_2
139	207	InterPro	IPR000014	PAS domain
17	87	SMART	SM00091	pas_2
17	87	InterPro	IPR000014	PAS domain
400	429	PRINTS	PR00260	Bacterial chemotaxis sensory transducer signature
400	429	InterPro	IPR004090	Chemotaxis methyl-accepting receptor
352	381	PRINTS	PR00260	Bacterial chemotaxis sensory transducer signature
352	381	InterPro	IPR004090	Chemotaxis methyl-accepting receptor
323	350	PRINTS	PR00260	Bacterial chemotaxis sensory transducer signature
323	350	InterPro	IPR004090	Chemotaxis methyl-accepting receptor
152	252	SUPERFAMILY	SSF55785	PYP-like sensor domain (PAS domain)
152	252	InterPro	IPR035965	PAS domain superfamily
144	252	Gene3D	G3DSA:3.30.450.20	PAS domain
226	431	SMART	SM00283	MA_2
226	431	InterPro	IPR004089	Methyl-accepting chemotaxis protein (MCP) signalling domain
150	260	NCBIfam	TIGR00229	PAS domain S-box protein
150	260	InterPro	IPR000014	PAS domain
29	134	NCBIfam	TIGR00229	PAS domain S-box protein
29	134	InterPro	IPR000014	PAS domain
211	263	ProSiteProfiles	PS50113	PAC domain profile.
211	263	InterPro	IPR000700	PAS-associated, C-terminal
151	251	CDD	cd00130	PAS
151	251	InterPro	IPR000014	PAS domain
253	430	Gene3D	G3DSA:1.10.287.950	-
16	143	Gene3D	G3DSA:3.30.450.20	PAS domain
259	431	ProSiteProfiles	PS50111	Bacterial chemotaxis sensory transducers domain profile.
259	431	InterPro	IPR004089	Methyl-accepting chemotaxis protein (MCP) signalling domain
298	427	Pfam	PF00015	Methyl-accepting chemotaxis protein (MCP) signalling domain
298	427	InterPro	IPR004089	Methyl-accepting chemotaxis protein (MCP) signalling domain
4	424	PANTHER	PTHR24422	CHEMOTAXIS PROTEIN METHYLTRANSFERASE
157	253	Pfam	PF13426	PAS domain
157	253	InterPro	IPR000014	PAS domain
29	131	CDD	cd00130	PAS
29	131	InterPro	IPR000014	PAS domain
92	134	SMART	SM00086	pac_2
92	134	InterPro	IPR001610	PAC motif
212	254	SMART	SM00086	pac_2
212	254	InterPro	IPR001610	PAC motif

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 PA1930	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				0.783
3				0.205

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.

37 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.

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
5DD	6I24	C5NSW6	457.4 Da LogP -0.88 TPSA 189.2	1 viol.	✓ Clean	`Cc1cc2c(cc1C)N(C3=NC(=O)NC(=O)[C@@H]3C2)C[C@@H]…`
9O9	6I23	C5NSW6	455.4 Da LogP -1.00 TPSA 195.2	1 viol.	✓ Clean	`Cc1cc2c(cc1C)N(C3=NC(=O)NC(=O)C3=C2)C[C@@H]([C@…`

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
ZINC5012547	1.000	455.4 Da LogP -1.00 TPSA 195.2	1 viol.	✓ Clean	`Cc1cc2cc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@H](O)[…`
ZINC1703511	0.745	375.4 Da LogP -1.12 TPSA 148.7	✓ Ro5	✓ Clean	`Cc1cc2cc3c(=O)[nH]c(=O)nc-3n(C[C@@H](O)[C@H](O)…`
ZINC4878448	0.745	375.4 Da LogP -1.12 TPSA 148.7	✓ Ro5	✓ Clean	`Cc1cc2cc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@H](O)[…`
ZINC4878449	0.745	375.4 Da LogP -1.12 TPSA 148.7	✓ Ro5	✓ Clean	`Cc1cc2cc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@@H](O)…`
ZINC4878453	0.745	375.4 Da LogP -1.12 TPSA 148.7	✓ Ro5	✓ Clean	`Cc1cc2cc3c(=O)[nH]c(=O)nc-3n(C[C@@H](O)[C@@H](O…`
ZINC3831425	0.721	456.3 Da LogP -1.61 TPSA 208.1	1 viol.	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@H](O)[…`
ZINC3831426	0.721	456.3 Da LogP -1.61 TPSA 208.1	1 viol.	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@@H](O)[C@H](O)…`
ZINC3831427	0.721	456.3 Da LogP -1.61 TPSA 208.1	1 viol.	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@@H](O)…`
ZINC3831428	0.721	456.3 Da LogP -1.61 TPSA 208.1	1 viol.	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@@H](O)[C@@H](O…`
ZINC8551105	0.721	456.3 Da LogP -1.61 TPSA 208.1	1 viol.	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@@H](O)[C@@H](O…`
ZINC8551106	0.721	456.3 Da LogP -1.61 TPSA 208.1	1 viol.	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@@H](O)…`
ZINC8551108	0.721	456.3 Da LogP -1.61 TPSA 208.1	1 viol.	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@H](O)[…`
ZINC100069844	0.556	363.3 Da LogP -2.03 TPSA 168.9	1 viol.	✓ Clean	`O=c1nc2n(C[C@H](O)[C@H](O)[C@H](O)CO)c3cc(O)ccc…`
ZINC4878473	0.548	347.3 Da LogP -1.74 TPSA 148.7	✓ Ro5	✓ Clean	`O=c1nc2n(C[C@H](O)[C@H](O)[C@H](O)CO)c3ccccc3cc…`
ZINC4878477	0.548	347.3 Da LogP -1.74 TPSA 148.7	✓ Ro5	✓ Clean	`O=c1nc2n(C[C@@H](O)[C@H](O)[C@H](O)CO)c3ccccc3c…`
ZINC4878479	0.548	347.3 Da LogP -1.74 TPSA 148.7	✓ Ro5	✓ Clean	`O=c1nc2n(C[C@H](O)[C@@H](O)[C@H](O)CO)c3ccccc3c…`
ZINC4878481	0.548	347.3 Da LogP -1.74 TPSA 148.7	✓ Ro5	✓ Clean	`O=c1nc2n(C[C@@H](O)[C@@H](O)[C@H](O)CO)c3ccccc3…`
ZINC1562485	0.524	374.4 Da LogP -0.51 TPSA 135.8	✓ Ro5	✓ Clean	`Cc1cc2cc3c(=O)[nH]c(=O)cc-3n(C[C@@H](O)[C@H](O)…`
ZINC5372514	0.524	374.4 Da LogP -0.51 TPSA 135.8	✓ Ro5	✓ Clean	`Cc1cc2cc3c(=O)[nH]c(=O)cc-3n(C[C@H](O)[C@H](O)[…`
ZINC5372517	0.524	374.4 Da LogP -0.51 TPSA 135.8	✓ Ro5	✓ Clean	`Cc1cc2cc3c(=O)[nH]c(=O)cc-3n(C[C@H](O)[C@@H](O)…`
ZINC5372519	0.524	374.4 Da LogP -0.51 TPSA 135.8	✓ Ro5	✓ Clean	`Cc1cc2cc3c(=O)[nH]c(=O)cc-3n(C[C@@H](O)[C@@H](O…`
ZINC1731984	0.523	392.4 Da LogP -2.49 TPSA 175.6	✓ Ro5	✓ Clean	`Cc1cc2c(cc1C)[n+]([O-])c1c(=O)[nH]c(=O)nc-1n2C[…`
ZINC5011745	0.523	392.4 Da LogP -2.49 TPSA 175.6	✓ Ro5	✓ Clean	`Cc1cc2c(cc1C)[n+]([O-])c1c(=O)[nH]c(=O)nc-1n2C[…`
ZINC5011746	0.523	392.4 Da LogP -2.49 TPSA 175.6	✓ Ro5	✓ Clean	`Cc1cc2c(cc1C)[n+]([O-])c1c(=O)[nH]c(=O)nc-1n2C[…`
ZINC5011747	0.523	392.4 Da LogP -2.49 TPSA 175.6	✓ Ro5	✓ Clean	`Cc1cc2c(cc1C)[n+]([O-])c1c(=O)[nH]c(=O)nc-1n2C[…`
ZINC13513101	0.522	456.4 Da LogP -1.90 TPSA 204.9	1 viol.	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@H](O)[…`
ZINC11565587	0.516	376.4 Da LogP -1.72 TPSA 161.6	✓ Ro5	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@@H](O)[C@H](O)…`
ZINC1532585	0.516	376.4 Da LogP -1.72 TPSA 161.6	✓ Ro5	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@@H](O)[C@@H](O…`
ZINC1769096	0.516	376.4 Da LogP -1.72 TPSA 161.6	✓ Ro5	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@H](O)[…`
ZINC2036848	0.516	376.4 Da LogP -1.72 TPSA 161.6	✓ Ro5	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@H](O)[…`
ZINC3650334	0.516	376.4 Da LogP -1.72 TPSA 161.6	✓ Ro5	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@@H](O)…`
ZINC3831422	0.516	376.4 Da LogP -1.72 TPSA 161.6	✓ Ro5	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@@H](O)[C@H](O)…`
ZINC3831423	0.516	376.4 Da LogP -1.72 TPSA 161.6	✓ Ro5	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@@H](O)…`
ZINC3831424	0.516	376.4 Da LogP -1.72 TPSA 161.6	✓ Ro5	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@@H](O)[C@@H](O…`
ZINC149168378	0.508	374.4 Da LogP -0.31 TPSA 141.3	✓ Ro5	✓ Clean	`CC[C@@H](O)[C@@H](O)[C@@H](O)Cn1c2nc(=O)[nH]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.