Protein profile

VK055_4177

evgS-Phis

Genome: KpATCC43816

Gene: AIK82722.1 evgS2 Structure source: AlphaFold + ColabFold UniProt A0A483MVK4

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Amino acids 1214

Annotations 9

Features 79

PDB binders 3

Druggability 0.734

Overview

Basic information about this protein and its source genome.

Accession: VK055_4177
Assembly: Klebsiella pneumoniae subsp. pneumoniae strain ATCC 43816 KPPR1, complete genome
Gene: AIK82722.1 evgS2
Status: annotated
Amino acids: 1214
Structure source: AlphaFold + ColabFold

2.7.13.3

GO:0016772 Catalysis of the transfer of a phosphorus-containing group from one compound (donor) to another (acceptor). 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: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: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: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. GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Human identity (%): 0.0
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 43.49
DEG E-value: 0.0
Localization: CytoplasmicMembrane
ColabFold pLDDT: 79.09

Selected Druggability evidence

AlphaFold / UniProt model

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 0.734

Structure A0A483MVK4

Pocket Pocket 1

P2Rank 0.935

Structure A0A483MVK4

Pocket Pocket 1

ColabFold model

FPocket 0.747 · Pocket 10

P2Rank 0.895 · Pocket 1

Core conservation Accessory gene

Roary accessory

CoreCruncher accessory

Gut microbiome 3 / 4744 genomes with a hit

Normalized 0.001

Sequence

Primary amino-acid sequence viewer.

MIIVLAMILLTGQTVAATTEPITLTLSSKKHNFISKLPLSQEDLAWLADKRTMTIAVYGEENPPIAMNSNNGCYRGINADYLQLLKDALHVNLVLHYYDDETQALSALNKEEADLVLTSNNTSHQATTPFIISQLLFQAYPTLVTLNSNGMMPFYQLDKTVNVAVSQHYPSDTFIKSIFRHANIVSYSSNYQALASVAKSENDYFIGDNIASNFLIARDFYQKLDIVKYWRSPLTGSYFIARENQSRLVEIINKFISALDASTHIRISHTWVDDGNLTFLTKPLSLTPKEKRWIEKNPVLRTLVNPYYAPFTVLDENREIRGLVGDILNLVQLQTGLHFQPVIAKSNSDMAEIMRKGDWDMVPTVTYSPEREDEMAFTQPFFSTPYVVVSRTENKQKDIFQAGSTVAIPAYYSLRDKLIQKYPDVHWIIVENTSTALSSLNLGKVDSVVTTQLAARYIIDHYYPETMSYQRIPNQPSAQIAFAVPRDKPELQSILNKALAEIPPKETLSLAGKWIKMPEVKIDTWDLYSRPFYILTVSAVLLILSSLLWGGYLLRAIRREKASQAALEYQLSLRQTLSNSIPVPVYITTPEGEIESYNRAFNAFFTPQQREAIHYSLFDRRSPLVHIFPVIQQEMQQGLAPDTVASHQFTLNNGAEDRTILHWMTLCPLPVPLPPVLICGWQDITESRKLMEALQVEKDKAIEASRAKSRFLARMSHEIRTPVSAIMGFLELLATGPQSEREAQESLQLAYATAQSLIGLIGDVLDMEKIESGNFELTPEWVDIEALTQATMANFAGLARQKNLQLTVSYQLNAGGILWLDPQAIKQVLANFLSNAIKFTVSGGVEIKVETQPRENDAAQLILSVKDSGVGISEEEQQLLFKPFSQASCGKKQMGSGLGLTICKELMDRMHGTISVASHPGTGTTMSIYVQTQVSDRAPADLNNQEMALPVSSGLRVIIADDNPTNRLLLRRQLDILGYYVDDVEDGEQAFSLIKRRQYDLLITDLNMPGMDGLTLAQQVRKINPALVIWGLTANAQPDEKARCLASGMDLCLIKPVNLPQLAAAFNSITQRLENPTQTEISASLNTPLDTTVCNELIDMQALRANAMDDTAFMLELINQAYHENVKDLAALKKAMFSHDRDIVRYHLHRINGTAQLIGATSLHVLADKLENALASEQPLSLFGEDMQLLEQQLIALGKAMDNFLKREGLTSRE

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Enzyme Commission (EC)

2.7.13.3

Gene Ontology (GO)

GO:0016772 Catalysis of the transfer of a phosphorus-containing group from one compound (donor) to another (acceptor).
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: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: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: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.
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:0009927 Serves as a phospho-His intermediate enabling the transfer of phospho group between a hybrid kinase and a response regulator.

Sequence Features

Domain/signature hits from InterPro and related databases.

79 records

Show feature table

Start	End	DB	Term	Name
60	272	Pfam	PF00497	Bacterial extracellular solute-binding proteins, family 3
60	272	InterPro	IPR001638	Solute-binding protein family 3/N-terminal domain of MltF
297	515	CDD	cd13707	PBP2_BvgS_D2
1	17	Phobius	SIGNAL_PEPTIDE	Signal peptide region
957	1065	CDD	cd17546	REC_hyHK_CKI1_RcsC-like
707	773	Pfam	PF00512	His Kinase A (phospho-acceptor) domain
707	773	InterPro	IPR003661	Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
290	514	Gene3D	G3DSA:3.40.190.10	-
705	769	CDD	cd00082	HisKA
705	769	InterPro	IPR003661	Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
50	272	CDD	cd13705	PBP2_BvgS_D1
54	273	SUPERFAMILY	SSF53850	Periplasmic binding protein-like II
684	704	Coils	Coil	Coil
1212	1214	Coils	Coil	Coil
956	1070	ProSiteProfiles	PS50110	Response regulatory domain profile.
956	1070	InterPro	IPR001789	Signal transduction response regulator, receiver domain
18	531	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
697	773	Gene3D	G3DSA:1.10.287.130	-
52	275	SMART	SM00062	AABind_6
52	275	InterPro	IPR001638	Solute-binding protein family 3/N-terminal domain of MltF
299	518	SMART	SM00062	AABind_6
299	518	InterPro	IPR001638	Solute-binding protein family 3/N-terminal domain of MltF
825	931	CDD	cd16922	HATPase_EvgS-ArcB-TorS-like
714	934	ProSiteProfiles	PS50109	Histidine kinase domain profile.
714	934	InterPro	IPR005467	Histidine kinase domain
300	517	SUPERFAMILY	SSF53850	Periplasmic binding protein-like II
1095	1208	Gene3D	G3DSA:1.20.120.160	HPT domain
1095	1208	InterPro	IPR036641	HPT domain superfamily
532	554	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
1	1	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
821	931	Pfam	PF02518	Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
821	931	InterPro	IPR003594	Histidine kinase/HSP90-like ATPase
953	1078	SUPERFAMILY	SSF52172	CheY-like
953	1078	InterPro	IPR011006	CheY-like superfamily
1049	1180	SUPERFAMILY	SSF47226	Histidine-containing phosphotransfer domain, HPT domain
1049	1180	InterPro	IPR036641	HPT domain superfamily
2	12	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
385	477	Gene3D	G3DSA:3.40.190.10	-
707	773	SMART	SM00388	HisKA_10
772	936	FunFam	G3DSA:3.30.565.10:FF:000010	Sensor histidine kinase RcsC
555	1214	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
532	554	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
894	912	PRINTS	PR00344	Bacterial sensor protein C-terminal signature
894	912	InterPro	IPR004358	Signal transduction histidine kinase-related protein, C-terminal
879	889	PRINTS	PR00344	Bacterial sensor protein C-terminal signature
879	889	InterPro	IPR004358	Signal transduction histidine kinase-related protein, C-terminal
918	931	PRINTS	PR00344	Bacterial sensor protein C-terminal signature
918	931	InterPro	IPR004358	Signal transduction histidine kinase-related protein, C-terminal
861	875	PRINTS	PR00344	Bacterial sensor protein C-terminal signature
861	875	InterPro	IPR004358	Signal transduction histidine kinase-related protein, C-terminal
1	16	SignalP_GRAM_NEGATIVE	SignalP-noTM	SignalP-noTM
774	939	Gene3D	G3DSA:3.30.565.10	-
774	939	InterPro	IPR036890	Histidine kinase/HSP90-like ATPase superfamily
301	514	Pfam	PF00497	Bacterial extracellular solute-binding proteins, family 3
301	514	InterPro	IPR001638	Solute-binding protein family 3/N-terminal domain of MltF
556	696	Gene3D	G3DSA:3.30.450.20	PAS domain
1122	1197	Pfam	PF01627	Hpt domain
1122	1197	InterPro	IPR008207	Signal transduction histidine kinase, phosphotransfer (Hpt) domain
139	234	Gene3D	G3DSA:3.40.190.10	-
490	1067	PANTHER	PTHR43047	TWO-COMPONENT HISTIDINE PROTEIN KINASE
659	681	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
557	685	SUPERFAMILY	SSF55785	PYP-like sensor domain (PAS domain)
557	685	InterPro	IPR035965	PAS domain superfamily
1110	1204	ProSiteProfiles	PS50894	Histidine-containing phosphotransfer (HPt) domain profile.
1110	1204	InterPro	IPR008207	Signal transduction histidine kinase, phosphotransfer (Hpt) domain
955	1066	SMART	SM00448	REC_2
955	1066	InterPro	IPR001789	Signal transduction response regulator, receiver domain
690	774	SUPERFAMILY	SSF47384	Homodimeric domain of signal transducing histidine kinase
690	774	InterPro	IPR036097	Signal transduction histidine kinase, dimerisation/phosphoacceptor domain superfamily
820	934	SMART	SM00387	HKATPase_4
820	934	InterPro	IPR003594	Histidine kinase/HSP90-like ATPase
42	271	Gene3D	G3DSA:3.40.190.10	-
940	1082	Gene3D	G3DSA:3.40.50.2300	-
957	1066	Pfam	PF00072	Response regulator receiver domain
957	1066	InterPro	IPR001789	Signal transduction response regulator, receiver domain
13	17	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
1	17	SignalP_GRAM_POSITIVE	SignalP-TM	SignalP-TM
763	930	SUPERFAMILY	SSF55874	ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
763	930	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.

Loading 3D structure...

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Structural evidence

0 + 2

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

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold AF_A0A483MVK4	AlphaFold	—	—	full sequence	—	Viewing
ColabFold VK055_4177	ColabFold	—	—	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				0.734
3				0.281
6				0.233

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	Score	Probability
1	22.95	0.885
2	7.92	0.421
3	5.87	0.287
4	2.75	0.083
5	2.6	0.075

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
10				0.747

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	Score	Probability
1	18.84	0.831
2	4.94	0.223
3	4.56	0.196
4	3.6	0.134
5	3.26	0.114

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.

53 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	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)…`
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`

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…`
ZINC1582675	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.