Protein target profile

PA0413

chemotactic signal transduction system protein

Genome: NC_002516.2

Gene: chpA PA0413 3D evidence: AlphaFold DB model UniProt Q9I696

Export view

Length 2472

Pocket druggability 0.691

Ligand records 55

EC / GO 1 / 9

Target summary

Target candidate with partial support; inspect missing evidence before prioritizing.

4 signals

Strengths

Risks / watch

No major risk signal surfaced in the loaded evidence.

Missing evidence

No metabolic context No SBML/network-derived reaction evidence is loaded for this protein.

How to read this page

PDB: experimentally determined structures from the Protein Data Bank. These are the strongest structural evidence, but may cover only part of the protein.

AlphaFold DB model: a precomputed predicted structure downloaded from AlphaFold Database/UniProt, not an experiment performed here.

ColabFold model: a predicted structure generated for this workspace; interpret it with coverage and confidence.

pLDDT: confidence score for predicted structures. High values support local geometry; low values mean the region should not drive pocket interpretation.

FPocket / P2Rank: software tools that predict possible ligand-binding pockets on a 3D structure. They are useful screening signals, not experimental validation.

Druggability: a pocket-based estimate of whether a small molecule could bind productively. It does not mean a drug already exists.

PDB ligand: a compound observed in an experimental structure. Direct same-protein records are stronger than homolog-transferred records.

ChEMBL: a public database of measured compound bioactivity. Direct entries are stronger than entries transferred from similar proteins.

ZINC: a purchasable-compound database. Here it marks proposed candidates from chemical similarity, not measured binders.

LigQ / LigQ_2: an internal TPW pipeline step that gathers PDB, ChEMBL, and ZINC ligand evidence for each protein.

Off-target: sequence similarity to proteins we prefer not to hit, such as human proteins or beneficial gut microbiome proteins.

DEG: Database of Essential Genes. A match suggests the protein resembles genes known to be essential in other organisms.

Roary / CoreCruncher: pan-genome tools used to decide whether a gene is core across analyzed strains or accessory/strain-specific.

EC / GO: functional annotations: EC describes enzyme reactions; GO describes biological process, molecular function, or cellular component.

KEGG pathway: a curated metabolic route label used here to group reactions imported from the metabolic model.

Chokepoint: a metabolic reaction that is the only producer or consumer of a metabolite in the imported model.

Overview

Basic information about this protein and its source genome.

Accession: PA0413
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: chpA PA0413
Status: annotated
Amino acids: 2472
3D evidence: AlphaFold DB model

2.7.13.3

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. 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: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: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:0050920 Any process that modulates the frequency, rate or extent of the directed movement of a motile cell or organism in response to a specific chemical concentration gradient. 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: Cytoplasmic

Selected pocket evidence

The selected pocket score is the FPocket value used for ranking after applying the curated structure priority. It estimates small-molecule pocket quality; it is not experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

FPocket 0.691

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MGDRHDYVALEWVKGEIAETLKQARQALEAFVENPQDPTRMRFCLTYVHQVQGTLQMVEFYGAALLAEEMEQLVQALLDGRVPNQGEALEVLMQAILQLPVYLDRIQTARRDLPMVVLPLLNDLRAARGEKLLSETSLFAPDLSQRQPQLDGEAIAQLRTDELGGLLRKLRQTQQMALVGLLRNQDVATSLGYLARVYARLEGLCREAPLGPLWSIASGLVEGLANGSVVNSASVRTLLRQLDRELKRLVEQGADGLNQAAPDELVKNLLFYVAKAPSQSPRIRALKEQYRLDEALPDHETVDAERARLAGPDRDAMRSVVGALCEELVRIKDSLDLFVRSDRGHPSELDALLAPLKQIADTLAVLGFGQPRKVILDQLDVIHALAQGRREPSDAILMDVAGALLYVEATLAGMAGPGDERNSEESRLPTTDVAQIHQLVIKEARNGLEQAKDAIIEFIASQWNHEHLARVPELLTQVRGGLAMIPLERAATLLETCNRYIQEQLLARKAVPDWQSLDTLADAITSVEYYLERLSEDHASQSDLILDVAEDSLANLGYTLKPNSSAPAEPGLSGPAAIESPAAEPERPEAVVEVAETAEQPPADTAPAEAAREDAPQLASDDNWTLGEVAPDAGEPSLDLALDLPLDDSAEVPPALPEVVEESGQPQSTSAPARSLDDFSLDEIDLSGLDLPADAAPASGPAALADWSLPEQWGLGDDLAQPAQAGETLDLSLEEPALSFDAPLESLEPLPALEPFDGSAEQELVLDALDPLPLDVALPEAEGEVSAWEGSSLEELDLSDLDLPEVQLPEAEAEAPPAAEALASEAPALSLAEVMAAPVQPINPPAQNVPVSLLPPPADEEPVDEELREVFIEEAGEVLETIGRYLPAWKADHDDREALTEVRRAFHTLKGSGRMVRALVIGELAWSIENLFNRVLDRSIAASEPVQRVVDQVVALLPELVEEFAANAQRQRDDVDLLAATAHALAKGEPLPEPPAPDDGGVPPEAGAEQPSSLDNGVQAPPLADAPQAAAEAQSDVELLDPQLLEIFTNEAETHLEALVGFLADCARELPQPVTDALQRALHTLKGSAHMAGILPIAEIATPLEKLVKEYKSNLLAFDLREAELLHDAEQLFRIGLEQVGAQRPLNPIPGSDALLERIEALHQERIASLEAERYSDAGERRDPLLIEAFLVEGMDILLDAEDLLERWHEHPQERQELSALREELSTLDRGARHAELPQVEELCQALLALYDAVEEGRLAVSPAFFEEARQAHEALIGMMDQVAAGLQVTPRPERVAALQELLEAPAAEAVPFIDPESLGADDFPPEDEEPALPEAVYEEAGAPAEETVPAAPAPAPGRELDEEMVSIFLEEAVDILESAGQALAQWQAEPGALSSLSALQRDLHTLKGGARMAEIAEIGDLAHELEALYEGLVDRRYQHSPQLAGLLQACHDRLAEQLDQLSAGQPLADPHDLIQSIRRFRQGPVAEAATPGEAESPVEELVAPAVEEPAAPAAEAFEERDPELVEIFLEEGFDILDSAAAALQRWMDDVDNTIELEALQRDLHTLKGGARMAEIGEIGDLAHELEFLYEGLCGGRLRASPALFGLLQRCHDELAEMLEAVRGHRTLPDGQALIAEIRRLRSDPDEQLSVPTSVSLKPLAAKGAAADESEILDIFLEEADDLLENLELALGRWDGGNGDAQPLDDLLRILHTLKGGARLAGQTELGNLAHDLEQHLTDAQQQGAPWPDSLLLDAQSGLEGLQRQVDLLRERLAEDDEAGERPEPAQALVQADDTDRAVASALAELTRLAPAAGAIMAAEAAPPAAPATTLPFVRKAQEAAQEAASRRAPQELVKVPAELLENLVNLAGETSIFRGRVEQQVSDVGFTLGEMESTIERVRDQLRRLDTETQAQILSRHQADAERAGYEEFDPLEMDRYSQLQQLSRALFESASDLLDLKETLAAKNRDAETLLLQQARVNTELQEGLMRTRMVPFDRLVPRLRRIVRQVAGELGKQVEFVVGNADGEMDRTVLERIVAPLEHMLRNAVDHGIESGETRRAAGKPEHGTIRLNIGREGGDILLTLSDDGAGIRLDAVRRKAIERGLMSADSDLSDHEVLQFVLESGFSTAEKVTQISGRGVGLDVANSEVKQLGGSVSIQTEPGQGTRFNVRLPFTVSVNRALMVLSGEDLYAVPLNTIEGIVRVSPYELEALYDQRGEAGLDTPSFEYAGQSYELKYLGELLNNGQEPKLVGQSLPLPVILVRSSEHAVAVQVDSLAGSREIVVKSLGPQFAGVAGISGATLLGDGRVVVILDLLATIRSRHALLGQESRRERLALRQEMAASESEQQRPPLVMVVDDSVTVRKVTTRLLERNGMNVLTAKDGVDAIAQLQEHRPDILLLDIEMPRMDGFEVATLVRHDERLGNLPIIMITSRTGEKHRERALGIGVNQYLGKPYQETELLEAIQSLVGQHE

MGDRHDYVALEWVKGEIAETLKQARQALEAFVENPQDPTRMRFCLTYVHQVQGTLQMVEFYGAALLAEEMEQLVQALLDGRVPNQGEALEVLMQAILQLPVYLDRIQTARRDLPMVVLPLLNDLRAARGEKLLSETSLFAPDLSQRQPQLDGEAIAQLRTDELGGLLRKLRQTQQMALVGLLRNQDVATSLGYLARVYARLEGLCREAPLGPLWSIASGLVEGLANGSVVNSASVRTLLRQLDRELKRLVEQGADGLNQAAPDELVKNLLFYVAKAPSQSPRIRALKEQYRLDEALPDHETVDAERARLAGPDRDAMRSVVGALCEELVRIKDSLDLFVRSDRGHPSELDALLAPLKQIADTLAVLGFGQPRKVILDQLDVIHALAQGRREPSDAILMDVAGALLYVEATLAGMAGPGDERNSEESRLPTTDVAQIHQLVIKEARNGLEQAKDAIIEFIASQWNHEHLARVPELLTQVRGGLAMIPLERAATLLETCNRYIQEQLLARKAVPDWQSLDTLADAITSVEYYLERLSEDHASQSDLILDVAEDSLANLGYTLKPNSSAPAEPGLSGPAAIESPAAEPERPEAVVEVAETAEQPPADTAPAEAAREDAPQLASDDNWTLGEVAPDAGEPSLDLALDLPLDDSAEVPPALPEVVEESGQPQSTSAPARSLDDFSLDEIDLSGLDLPADAAPASGPAALADWSLPEQWGLGDDLAQPAQAGETLDLSLEEPALSFDAPLESLEPLPALEPFDGSAEQELVLDALDPLPLDVALPEAEGEVSAWEGSSLEELDLSDLDLPEVQLPEAEAEAPPAAEALASEAPALSLAEVMAAPVQPINPPAQNVPVSLLPPPADEEPVDEELREVFIEEAGEVLETIGRYLPAWKADHDDREALTEVRRAFHTLKGSGRMVRALVIGELAWSIENLFNRVLDRSIAASEPVQRVVDQVVALLPELVEEFAANAQRQRDDVDLLAATAHALAKGEPLPEPPAPDDGGVPPEAGAEQPSSLDNGVQAPPLADAPQAAAEAQSDVELLDPQLLEIFTNEAETHLEALVGFLADCARELPQPVTDALQRALHTLKGSAHMAGILPIAEIATPLEKLVKEYKSNLLAFDLREAELLHDAEQLFRIGLEQVGAQRPLNPIPGSDALLERIEALHQERIASLEAERYSDAGERRDPLLIEAFLVEGMDILLDAEDLLERWHEHPQERQELSALREELSTLDRGARHAELPQVEELCQALLALYDAVEEGRLAVSPAFFEEARQAHEALIGMMDQVAAGLQVTPRPERVAALQELLEAPAAEAVPFIDPESLGADDFPPEDEEPALPEAVYEEAGAPAEETVPAAPAPAPGRELDEEMVSIFLEEAVDILESAGQALAQWQAEPGALSSLSALQRDLHTLKGGARMAEIAEIGDLAHELEALYEGLVDRRYQHSPQLAGLLQACHDRLAEQLDQLSAGQPLADPHDLIQSIRRFRQGPVAEAATPGEAESPVEELVAPAVEEPAAPAAEAFEERDPELVEIFLEEGFDILDSAAAALQRWMDDVDNTIELEALQRDLHTLKGGARMAEIGEIGDLAHELEFLYEGLCGGRLRASPALFGLLQRCHDELAEMLEAVRGHRTLPDGQALIAEIRRLRSDPDEQLSVPTSVSLKPLAAKGAAADESEILDIFLEEADDLLENLELALGRWDGGNGDAQPLDDLLRILHTLKGGARLAGQTELGNLAHDLEQHLTDAQQQGAPWPDSLLLDAQSGLEGLQRQVDLLRERLAEDDEAGERPEPAQALVQADDTDRAVASALAELTRLAPAAGAIMAAEAAPPAAPATTLPFVRKAQEAAQEAASRRAPQELVKVPAELLENLVNLAGETSIFRGRVEQQVSDVGFTLGEMESTIERVRDQLRRLDTETQAQILSRHQADAERAGYEEFDPLEMDRYSQLQQLSRALFESASDLLDLKETLAAKNRDAETLLLQQARVNTELQEGLMRTRMVPFDRLVPRLRRIVRQVAGELGKQVEFVVGNADGEMDRTVLERIVAPLEHMLRNAVDHGIESGETRRAAGKPEHGTIRLNIGREGGDILLTLSDDGAGIRLDAVRRKAIERGLMSADSDLSDHEVLQFVLESGFSTAEKVTQISGRGVGLDVANSEVKQLGGSVSIQTEPGQGTRFNVRLPFTVSVNRALMVLSGEDLYAVPLNTIEGIVRVSPYELEALYDQRGEAGLDTPSFEYAGQSYELKYLGELLNNGQEPKLVGQSLPLPVILVRSSEHAVAVQVDSLAGSREIVVKSLGPQFAGVAGISGATLLGDGRVVVILDLLATIRSRHALLGQESRRERLALRQEMAASESEQQRPPLVMVVDDSVTVRKVTTRLLERNGMNVLTAKDGVDAIAQLQEHRPDILLLDIEMPRMDGFEVATLVRHDERLGNLPIIMITSRTGEKHRERALGIGVNQYLGKPYQETELLEAIQSLVGQHE

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Enzyme Commission (EC)

2.7.13.3

Gene Ontology (GO)

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
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: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: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:0050920 Any process that modulates the frequency, rate or extent of the directed movement of a motile cell or organism in response to a specific chemical concentration gradient.
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:0004673 Catalysis of the reaction: ATP + protein L-histidine = ADP + protein phospho-L-histidine.
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.

119 records

Show feature table

Start	End	DB	Term	Name
565	686	MobiDBLite	mobidb-lite	consensus disorder prediction
1670	1774	CDD	cd00088	HPT
1670	1774	InterPro	IPR008207	Signal transduction histidine kinase, phosphotransfer (Hpt) domain
2352	2468	ProSiteProfiles	PS50110	Response regulatory domain profile.
2352	2468	InterPro	IPR001789	Signal transduction response regulator, receiver domain
1041	1164	SUPERFAMILY	SSF47226	Histidine-containing phosphotransfer domain, HPT domain
1041	1164	InterPro	IPR036641	HPT domain superfamily
1522	1644	SUPERFAMILY	SSF47226	Histidine-containing phosphotransfer domain, HPT domain
1522	1644	InterPro	IPR036641	HPT domain superfamily
1184	1304	SUPERFAMILY	SSF47226	Histidine-containing phosphotransfer domain, HPT domain
1184	1304	InterPro	IPR036641	HPT domain superfamily
2175	2314	SUPERFAMILY	SSF50341	CheW-like
2175	2314	InterPro	IPR036061	CheW-like domain superfamily
1358	1462	ProSiteProfiles	PS50894	Histidine-containing phosphotransfer (HPt) domain profile.
1358	1462	InterPro	IPR008207	Signal transduction histidine kinase, phosphotransfer (Hpt) domain
2181	2320	Pfam	PF01584	CheW-like domain
2181	2320	InterPro	IPR002545	CheW-like domain
1992	2173	SUPERFAMILY	SSF55874	ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
1992	2173	InterPro	IPR036890	Histidine kinase/HSP90-like ATPase superfamily
2178	2323	ProSiteProfiles	PS50851	CheW-like domain profile.
2178	2323	InterPro	IPR002545	CheW-like domain
2168	2318	SMART	SM00260	chew_2
2168	2318	InterPro	IPR002545	CheW-like domain
1670	1778	SUPERFAMILY	SSF47226	Histidine-containing phosphotransfer domain, HPT domain
1670	1778	InterPro	IPR036641	HPT domain superfamily
1991	2175	FunFam	G3DSA:3.30.565.10:FF:000016	Chemotaxis protein CheA, putative
2136	2154	PRINTS	PR00344	Bacterial sensor protein C-terminal signature
2136	2154	InterPro	IPR004358	Signal transduction histidine kinase-related protein, C-terminal
2080	2094	PRINTS	PR00344	Bacterial sensor protein C-terminal signature
2080	2094	InterPro	IPR004358	Signal transduction histidine kinase-related protein, C-terminal
2160	2173	PRINTS	PR00344	Bacterial sensor protein C-terminal signature
2160	2173	InterPro	IPR004358	Signal transduction histidine kinase-related protein, C-terminal
1362	1459	SMART	SM00073	hpt_2
1362	1459	InterPro	IPR008207	Signal transduction histidine kinase, phosphotransfer (Hpt) domain
1522	1619	SMART	SM00073	hpt_2
1522	1619	InterPro	IPR008207	Signal transduction histidine kinase, phosphotransfer (Hpt) domain
1669	1766	SMART	SM00073	hpt_2
1669	1766	InterPro	IPR008207	Signal transduction histidine kinase, phosphotransfer (Hpt) domain
864	961	SMART	SM00073	hpt_2
864	961	InterPro	IPR008207	Signal transduction histidine kinase, phosphotransfer (Hpt) domain
1041	1144	SMART	SM00073	hpt_2
1041	1144	InterPro	IPR008207	Signal transduction histidine kinase, phosphotransfer (Hpt) domain
1185	1312	Gene3D	G3DSA:1.20.120.160	HPT domain
1185	1312	InterPro	IPR036641	HPT domain superfamily
1522	1651	Gene3D	G3DSA:1.20.120.160	HPT domain
1522	1651	InterPro	IPR036641	HPT domain superfamily
14	137	Gene3D	G3DSA:1.20.120.160	HPT domain
14	137	InterPro	IPR036641	HPT domain superfamily
1522	1622	ProSiteProfiles	PS50894	Histidine-containing phosphotransfer (HPt) domain profile.
1522	1622	InterPro	IPR008207	Signal transduction histidine kinase, phosphotransfer (Hpt) domain
1998	2173	CDD	cd16916	HATPase_CheA-like
2353	2465	Pfam	PF00072	Response regulator receiver domain
2353	2465	InterPro	IPR001789	Signal transduction response regulator, receiver domain
7	130	SUPERFAMILY	SSF47226	Histidine-containing phosphotransfer domain, HPT domain
7	130	InterPro	IPR036641	HPT domain superfamily
1889	1909	Coils	Coil	Coil
1037	1143	ProSiteProfiles	PS50894	Histidine-containing phosphotransfer (HPt) domain profile.
1037	1143	InterPro	IPR008207	Signal transduction histidine kinase, phosphotransfer (Hpt) domain
1362	1492	Gene3D	G3DSA:1.20.120.160	HPT domain
1362	1492	InterPro	IPR036641	HPT domain superfamily
864	994	Gene3D	G3DSA:1.20.120.160	HPT domain
864	994	InterPro	IPR036641	HPT domain superfamily
2256	2316	Gene3D	G3DSA:2.30.30.40	SH3 Domains
1665	1769	ProSiteProfiles	PS50894	Histidine-containing phosphotransfer (HPt) domain profile.
1665	1769	InterPro	IPR008207	Signal transduction histidine kinase, phosphotransfer (Hpt) domain
1943	2176	ProSiteProfiles	PS50109	Histidine kinase domain profile.
1943	2176	InterPro	IPR005467	Histidine kinase domain
1041	1132	CDD	cd00088	HPT
1041	1132	InterPro	IPR008207	Signal transduction histidine kinase, phosphotransfer (Hpt) domain
1752	1779	Coils	Coil	Coil
1370	1390	Coils	Coil	Coil
2350	2469	SUPERFAMILY	SSF52172	CheY-like
2350	2469	InterPro	IPR011006	CheY-like superfamily
2353	2464	CDD	cd17546	REC_hyHK_CKI1_RcsC-like
1522	1620	CDD	cd00088	HPT
1522	1620	InterPro	IPR008207	Signal transduction histidine kinase, phosphotransfer (Hpt) domain
1756	2471	PANTHER	PTHR43395	SENSOR HISTIDINE KINASE CHEA
1989	2175	Gene3D	G3DSA:3.30.565.10	-
1989	2175	InterPro	IPR036890	Histidine kinase/HSP90-like ATPase superfamily
1362	1460	CDD	cd00088	HPT
1362	1460	InterPro	IPR008207	Signal transduction histidine kinase, phosphotransfer (Hpt) domain
860	967	ProSiteProfiles	PS50894	Histidine-containing phosphotransfer (HPt) domain profile.
860	967	InterPro	IPR008207	Signal transduction histidine kinase, phosphotransfer (Hpt) domain
864	960	CDD	cd00088	HPT
864	960	InterPro	IPR008207	Signal transduction histidine kinase, phosphotransfer (Hpt) domain
2035	2176	SMART	SM00387	HKATPase_4
2035	2176	InterPro	IPR003594	Histidine kinase/HSP90-like ATPase
232	252	Coils	Coil	Coil
1851	1990	SMART	SM01231	H_kinase_dim_2
1851	1990	InterPro	IPR004105	Histidine kinase CheA-like, homodimeric domain
1362	1484	SUPERFAMILY	SSF47226	Histidine-containing phosphotransfer domain, HPT domain
1362	1484	InterPro	IPR036641	HPT domain superfamily
715	737	MobiDBLite	mobidb-lite	consensus disorder prediction
2351	2464	SMART	SM00448	REC_2
2351	2464	InterPro	IPR001789	Signal transduction response regulator, receiver domain
1043	1129	Pfam	PF01627	Hpt domain
1043	1129	InterPro	IPR008207	Signal transduction histidine kinase, phosphotransfer (Hpt) domain
1524	1623	Pfam	PF01627	Hpt domain
1524	1623	InterPro	IPR008207	Signal transduction histidine kinase, phosphotransfer (Hpt) domain
10	98	Pfam	PF01627	Hpt domain
10	98	InterPro	IPR008207	Signal transduction histidine kinase, phosphotransfer (Hpt) domain
1671	1764	Pfam	PF01627	Hpt domain
1671	1764	InterPro	IPR008207	Signal transduction histidine kinase, phosphotransfer (Hpt) domain
1364	1457	Pfam	PF01627	Hpt domain
1364	1457	InterPro	IPR008207	Signal transduction histidine kinase, phosphotransfer (Hpt) domain
866	953	Pfam	PF01627	Hpt domain
866	953	InterPro	IPR008207	Signal transduction histidine kinase, phosphotransfer (Hpt) domain
864	989	SUPERFAMILY	SSF47226	Histidine-containing phosphotransfer domain, HPT domain
864	989	InterPro	IPR036641	HPT domain superfamily
1035	1170	Gene3D	G3DSA:1.20.120.160	HPT domain
1035	1170	InterPro	IPR036641	HPT domain superfamily
1663	1796	Gene3D	G3DSA:1.20.120.160	HPT domain
1663	1796	InterPro	IPR036641	HPT domain superfamily
433	556	SUPERFAMILY	SSF47226	Histidine-containing phosphotransfer domain, HPT domain
433	556	InterPro	IPR036641	HPT domain superfamily
2353	2472	Gene3D	G3DSA:3.40.50.2300	-
2039	2175	Pfam	PF02518	Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
2039	2175	InterPro	IPR003594	Histidine kinase/HSP90-like ATPase
981	1035	MobiDBLite	mobidb-lite	consensus disorder prediction

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; AlphaFold DB and ColabFold models typically cover the full protein but remain computational predictions.

Loading 3D structure...

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Structural evidence

0 + 1

Experimental PDB entries plus predicted AlphaFold DB or ColabFold models. Click Switch to display a different loaded structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold DB PA0413	AlphaFold DB	—	—	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
5				0.691
2				0.238

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

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 55 via homologs

Structural ligands 5 0 loaded crystals

Bioactive compounds 0 50 ZINC proposed compounds

Drug-like & clean 22 0 PAINS alerts

Best available ligand signal

ACP PDB via homolog 505.2 Da · LogP -1.52 · TPSA 269.9 Open detail RCSB PDB

Detail RCSB PDB ACP PDB via homolog

Detail RCSB PDB ANP PDB via homolog

Detail RCSB PDB BEF PDB via homolog

Detail RCSB PDB JSJ PDB via homolog

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
ACP RCSB PDB	1I58	Q56310	505.2 Da LogP -1.52 TPSA 269.9	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
ANP RCSB PDB	1I59	Q56310	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)…`
BEF RCSB PDB	6EB7	A0A0H2UQ68	66.0 Da LogP 0.88 TPSA 0.0	✓ Ro5	✓ Clean	`[Be-](F)(F)F`
JSJ RCSB PDB	6MI6	Q56310	628.6 Da LogP 1.83 TPSA 235.8	3 viol.	✓ Clean	`CC1(C=C(C(N1O)(C)C)CSSP(=O)(O)OP(=O)(O)OC[C@@H]…`
PHS RCSB PDB	1NXP	A0A0H2UQ68	82.0 Da LogP -0.64 TPSA 57.5	✓ Ro5	✓ Clean	`OP(=O)O`

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
ZINC105469665 ZINC	0.873	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)CP(=O…`
ZINC13527614 ZINC	0.873	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)CP(=O)…`
ZINC219330894 ZINC	0.873	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873852 ZINC	0.873	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873853 ZINC	0.873	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@](=O)(O)CP(=O…`
ZINC3873854 ZINC	0.873	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873855 ZINC	0.873	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@](=O)(O)CP(=O…`
ZINC12360002 ZINC	0.839	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12360703 ZINC	0.839	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12503599 ZINC	0.839	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC16546165 ZINC	0.839	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@](=O)(O)OP(=O)(…`
ZINC31977053 ZINC	0.839	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC4806433 ZINC	0.839	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC53683898 ZINC	0.839	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586019 ZINC	0.839	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC8586020 ZINC	0.839	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586021 ZINC	0.839	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)OP(=O…`
ZINC8586022 ZINC	0.839	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC13518964 ZINC	0.768	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC1532515 ZINC	0.768	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@H](O…`
ZINC1571045 ZINC	0.768	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC1842158 ZINC	0.768	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@H](O…`
ZINC2046931 ZINC	0.768	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC2126310 ZINC	0.768	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3201891 ZINC	0.768	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC3201893 ZINC	0.768	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3830180 ZINC	0.768	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3860156 ZINC	0.768	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3977897 ZINC	0.768	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](COP(=O)(O)O)[C@@H](O…`
ZINC4806442 ZINC	0.768	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC8613167 ZINC	0.768	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC4096224 ZINC	0.754	346.2 Da LogP -1.90 TPSA 191.9	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](N)(=O)O)[C@@…`
ZINC12503850 ZINC	0.750	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC141161066 ZINC	0.750	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC141163786 ZINC	0.750	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC4228246 ZINC	0.750	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OS(=O…`
ZINC105372833 ZINC	0.737	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@H](O…`
ZINC105372837 ZINC	0.737	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@H](O…`
ZINC17107643 ZINC	0.737	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC204538551 ZINC	0.737	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC31475423 ZINC	0.726	434.3 Da LogP -2.99 TPSA 238.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@@](=O)(O)OC(=O)…`
ZINC1532902 ZINC	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@@](O)(CC(=O)O)C(=O)O`
ZINC2018106 ZINC	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@](O)(CC(=O)O)C(=O)O`
ZINC5615251 ZINC	0.700	375.3 Da LogP -0.55 TPSA 164.1	1 viol.	✓ Clean	`COP(=O)(OC)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@…`
ZINC5615253 ZINC	0.700	375.3 Da LogP -0.55 TPSA 164.1	1 viol.	✓ Clean	`COP(=O)(OC)OC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)[C…`
ZINC5615258 ZINC	0.700	375.3 Da LogP -0.55 TPSA 164.1	1 viol.	✓ Clean	`COP(=O)(OC)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@…`
ZINC5615263 ZINC	0.700	375.3 Da LogP -0.55 TPSA 164.1	1 viol.	✓ Clean	`COP(=O)(OC)OC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)[C…`
ZINC31516918 ZINC	0.692	446.4 Da LogP -1.33 TPSA 218.2	1 viol.	✓ Clean	`CC(C)[C@H](N)C(=O)O[P@](=O)(O)OC[C@H]1O[C@@H](n…`
ZINC5486734 ZINC	0.689	403.3 Da LogP 0.23 TPSA 164.1	1 viol.	✓ Clean	`CCOP(=O)(OCC)OC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)…`
ZINC5486740 ZINC	0.689	403.3 Da LogP 0.23 TPSA 164.1	1 viol.	✓ Clean	`CCOP(=O)(OCC)OC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)…`

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.