Protein profile

PA3946

two-component sensor

Genome: NC_002516.2

Gene: rocS1 PA3946 Structure source: AlphaFold UniProt Q9HX70

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Amino acids 1212

Annotations 8

Features 94

PDB binders 5

Druggability 0.637

Overview

Basic information about this protein and its source genome.

Accession: PA3946
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: rocS1 PA3946
Status: annotated
Amino acids: 1212
Structure source: AlphaFold

2.7.13.3

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: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: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): 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 0.637

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MRSKLFLLFFCLLLSGGRLFAVEAHPSLTLFSQLRIEHEDMAIAEDDWAWLRHKGHLRLGAALDETSPFNVRLDDENYEGITADVATLVGQLLGMRIKVVSFDTHADAVAALAAGKIDLLGSHYSSAGDSSLVLSQPYARDRLAVFKRMGEKRNSPEDLAGLSVAVAREHVGELRQRFPRARFVVFGSHDEAVAAVAFGHTDLYLDDVLSAYHRINRSYYGYVRFERFADARLEGGYGFLLRRGDTNLLRVVNSAIGAINQDRLESIARRWVGSGSLPTGQRIALTPQESRWIARHPVVRLVINDDLAPLAFFNSDETFSGIASDLLDMISRRTGLHFQVTPRSGGFPEQIGVLARKEADLAIMSRSSKREEMLRFTRSFLSTSYVLVTRADDKGRAEIPGSLDGKRIAIPAGHVGMQQVRERYPQASMVEVGVALDAMNLVYEGRADAAVVPLVTARYYIVRLFRERLAIADLVPIGAATAHFAVRRGDAELQSILDKALLSISPDDLSDIVNRWRSPPGMSGQTWVDYILVITEILAIAAALLLLCLGWVTYQRRQIRVRARVEQALSDQLRFVEALTDCMPPPLYVRDVNGRMLSCNRSYLQSVGLSSEEVMNRTVLELPMENFETAPEFHRSYLMAMREGRTIEAVYPVALGGRERWIDHWIQPFRDSSGTIRGVICGWLDITEHRQLIDELEEAKNLADEASRAKTTFLATMSHEIRTPMNAVIGILELALKRAETGRVDRSSIEIAYASAKSLLELIGDILDIARIESGRLSLSPKRANLRELVESVARVFEGLARQKRLSLVLEIDSSINGDVLLDAMRFKQILSNLVSNAIKFTDEGSIRIRIDGRQVEPSLLQVNLCVEDTGIGISLGDQQQLFRPFAQVNRNLQNTEGTGLGLVISRSLCEMMGGRLVMSSELGQGTRIDVELRLQVLEPIVENVRAIPLGSRQARRLQVLVVDDHAVNRQILHQQLSFLGHDVEEAENGLSALNLWHGQPFDMVITDCHMPLMSGSDLARSIRQEERENGEEPVVIIGLTADAQPEEIERCIQAGMNECLIKPIGLDVLEERLLALGFAADELPVTIDAEPVAIPTAPRLYDLDSLHALTGGEPTMLRRLLDELLTSNRKDLETLEGLVQRQETGELAELAHRIKGAARVVRGEQLVESCRRLEDACLSPNASFAWVEECAVGVKLAILALDESLVEECTD

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Enzyme Commission (EC)

2.7.13.3

Gene Ontology (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: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: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.

94 records

Show feature table

Start	End	DB	Term	Name
469	486	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
1	24	SignalP_EUK	SignalP-noTM	SignalP-noTM
960	1074	Pfam	PF00072	Response regulator receiver domain
960	1074	InterPro	IPR001789	Signal transduction response regulator, receiver domain
716	937	ProSiteProfiles	PS50109	Histidine kinase domain profile.
716	937	InterPro	IPR005467	Histidine kinase domain
958	1074	SMART	SM00448	REC_2
958	1074	InterPro	IPR001789	Signal transduction response regulator, receiver domain
22	526	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
1	20	SignalP_GRAM_NEGATIVE	SignalP-noTM	SignalP-noTM
64	273	Pfam	PF00497	Bacterial extracellular solute-binding proteins, family 3
64	273	InterPro	IPR001638	Solute-binding protein family 3/N-terminal domain of MltF
686	709	Coils	Coil	Coil
1119	1178	CDD	cd00088	HPT
1119	1178	InterPro	IPR008207	Signal transduction histidine kinase, phosphotransfer (Hpt) domain
583	686	CDD	cd00130	PAS
583	686	InterPro	IPR000014	PAS domain
774	939	FunFam	G3DSA:3.30.565.10:FF:000010	Sensor histidine kinase RcsC
577	692	NCBIfam	TIGR00229	PAS domain S-box protein
577	692	InterPro	IPR000014	PAS domain
960	1074	CDD	cd17546	REC_hyHK_CKI1_RcsC-like
1057	1182	SUPERFAMILY	SSF47226	Histidine-containing phosphotransfer domain, HPT domain
1057	1182	InterPro	IPR036641	HPT domain superfamily
289	516	Gene3D	G3DSA:3.40.190.10	-
574	642	SMART	SM00091	pas_2
574	642	InterPro	IPR000014	PAS domain
709	775	Pfam	PF00512	His Kinase A (phospho-acceptor) domain
709	775	InterPro	IPR003661	Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
54	272	CDD	cd13705	PBP2_BvgS_D1
707	771	CDD	cd00082	HisKA
707	771	InterPro	IPR003661	Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
1114	1212	ProSiteProfiles	PS50894	Histidine-containing phosphotransfer (HPt) domain profile.
1114	1212	InterPro	IPR008207	Signal transduction histidine kinase, phosphotransfer (Hpt) domain
561	687	SUPERFAMILY	SSF55785	PYP-like sensor domain (PAS domain)
561	687	InterPro	IPR035965	PAS domain superfamily
532	554	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
141	234	Gene3D	G3DSA:3.40.190.10	-
5	22	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
1	4	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
560	698	Gene3D	G3DSA:3.30.450.20	PAS domain
863	877	PRINTS	PR00344	Bacterial sensor protein C-terminal signature
863	877	InterPro	IPR004358	Signal transduction histidine kinase-related protein, C-terminal
897	915	PRINTS	PR00344	Bacterial sensor protein C-terminal signature
897	915	InterPro	IPR004358	Signal transduction histidine kinase-related protein, C-terminal
881	891	PRINTS	PR00344	Bacterial sensor protein C-terminal signature
881	891	InterPro	IPR004358	Signal transduction histidine kinase-related protein, C-terminal
921	934	PRINTS	PR00344	Bacterial sensor protein C-terminal signature
921	934	InterPro	IPR004358	Signal transduction histidine kinase-related protein, C-terminal
527	554	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
5	16	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
709	775	SMART	SM00388	HisKA_10
645	698	ProSiteProfiles	PS50113	PAC domain profile.
645	698	InterPro	IPR000700	PAS-associated, C-terminal
1	21	Phobius	SIGNAL_PEPTIDE	Signal peptide region
956	1076	SUPERFAMILY	SSF52172	CheY-like
956	1076	InterPro	IPR011006	CheY-like superfamily
296	517	CDD	cd13707	PBP2_BvgS_D2
1121	1178	Pfam	PF01627	Hpt domain
1121	1178	InterPro	IPR008207	Signal transduction histidine kinase, phosphotransfer (Hpt) domain
46	271	Gene3D	G3DSA:3.40.190.10	-
1	21	SignalP_GRAM_POSITIVE	SignalP-TM	SignalP-TM
823	935	Pfam	PF02518	Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
823	935	InterPro	IPR003594	Histidine kinase/HSP90-like ATPase
56	275	SMART	SM00062	AABind_6
56	275	InterPro	IPR001638	Solute-binding protein family 3/N-terminal domain of MltF
298	520	SMART	SM00062	AABind_6
298	520	InterPro	IPR001638	Solute-binding protein family 3/N-terminal domain of MltF
292	519	SUPERFAMILY	SSF53850	Periplasmic binding protein-like II
692	776	SUPERFAMILY	SSF47384	Homodimeric domain of signal transducing histidine kinase
692	776	InterPro	IPR036097	Signal transduction histidine kinase, dimerisation/phosphoacceptor domain superfamily
17	21	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
777	940	Gene3D	G3DSA:3.30.565.10	-
777	940	InterPro	IPR036890	Histidine kinase/HSP90-like ATPase superfamily
765	935	SUPERFAMILY	SSF55874	ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
765	935	InterPro	IPR036890	Histidine kinase/HSP90-like ATPase superfamily
959	1078	ProSiteProfiles	PS50110	Response regulatory domain profile.
959	1078	InterPro	IPR001789	Signal transduction response regulator, receiver domain
1100	1205	Gene3D	G3DSA:1.20.120.160	HPT domain
1100	1205	InterPro	IPR036641	HPT domain superfamily
583	690	Pfam	PF08448	PAS fold
583	690	InterPro	IPR013656	PAS fold-4
572	622	ProSiteProfiles	PS50112	PAS repeat profile.
572	622	InterPro	IPR000014	PAS domain
684	936	PANTHER	PTHR45339	HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J
699	776	Gene3D	G3DSA:1.10.287.130	-
48	274	SUPERFAMILY	SSF53850	Periplasmic binding protein-like II
952	1076	Gene3D	G3DSA:3.40.50.2300	-
822	937	SMART	SM00387	HKATPase_4
822	937	InterPro	IPR003594	Histidine kinase/HSP90-like ATPase
299	516	Pfam	PF00497	Bacterial extracellular solute-binding proteins, family 3
299	516	InterPro	IPR001638	Solute-binding protein family 3/N-terminal domain of MltF
827	935	CDD	cd16922	HATPase_EvgS-ArcB-TorS-like
555	1212	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
384	479	Gene3D	G3DSA:3.40.190.10	-

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 PA3946	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				0.637
4				0.402

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

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
ANP	6QRJ	Q9ABT2	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	5N2N	O22267	66.0 Da LogP 0.88 TPSA 0.0	✓ Ro5	✓ Clean	`[Be-](F)(F)F`
BTB	3IQT	P0AEC6	209.2 Da LogP -3.01 TPSA 104.4	✓ Ro5	✓ Clean	`C(CO)N(CCO)C(CO)(CO)CO`
MBN	5HWV	A5W4E3	92.1 Da LogP 2.00 TPSA 0.0	✓ Ro5	✓ Clean	`Cc1ccccc1`
XBZ	5HWW	A5W4E3	120.2 Da LogP 2.61 TPSA 0.0	✓ Ro5	✓ Clean	`Cc1ccc(c(c1)C)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
ZINC1615342	1.000	209.2 Da LogP -3.01 TPSA 104.4	✓ Ro5	✓ Clean	`OCCN(CCO)C(CO)(CO)CO`
ZINC12360002	0.810	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	0.810	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	0.810	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	0.810	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	0.810	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	0.810	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	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586019	0.810	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	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586021	0.810	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	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC13518964	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC1532515	0.741	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	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC1842158	0.741	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	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC2126310	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3201891	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC3201893	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3830180	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3860156	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3977897	0.741	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	0.741	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	0.741	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	0.729	346.2 Da LogP -1.90 TPSA 191.9	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](N)(=O)O)[C@@…`
ZINC12503850	0.726	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	0.726	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	0.726	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	0.726	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	0.712	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	0.712	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	0.712	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC204538551	0.712	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC31475423	0.703	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	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	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`
ZINC105469665	0.694	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	0.694	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	0.694	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	0.694	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	0.694	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	0.694	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	0.694	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@](=O)(O)CP(=O…`
ZINC5615251	0.677	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	0.677	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	0.677	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	0.677	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	0.672	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…`
ZINC5486740	0.667	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.