Protein profile

PA2302

protein AmbE

Genome: NC_002516.2

Gene: ambE PA2302 Structure source: Experimental + AlphaFold UniProt Q9I1H3

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Amino acids 2124

Annotations 7

Features 65

PDB binders 7

Druggability 0.871

Overview

Basic information about this protein and its source genome.

Accession: PA2302
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: ambE PA2302
Status: annotated
Amino acids: 2124
Structure source: Experimental + AlphaFold

6.2.1.68

GO:0016405 Catalysis of the reaction: substrate + ATP + CoASH = AMP + diphosphate + substrate-CoA. GO:0031177 Binding to phosphopantetheine, the vitamin pantetheine 4'-(dihydrogen phosphate). GO:0006631 The chemical reactions and pathways involving fatty acids, aliphatic monocarboxylic acids liberated from naturally occurring fats and oils by hydrolysis. GO:0044550 The chemical reactions and pathways resulting in the formation of secondary metabolites, the compounds that are not necessarily required for growth and maintenance of cells, and are often unique to a taxon. GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic. GO:0009058 A cellular process consisting of the biochemical pathways by which a living organism synthesizes chemical substances. This typically represents the energy-requiring part of metabolism in which simpler substances are transformed into more complex ones.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 46.429
Human E-value: 1.76e-07
Gut microbiome off-target: hit
Essential (DEG): N
Localization: Cytoplasmic

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 0.871

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MSASEDLQSAVQPAASEALEGFPLSPLQTRAWRRHAERPENTVVGVRLHAPADPVATLERLRRALDGEAQLRVAYRTMPGMSLPVQVLDGRAADLLVERLPGDGDWAGRFARESARLAASPLGGEGQPVLALGLLLDAAGETLQGLLLAAPAFVVDAASLVALLRRGLGPAGQASADEGDEALLFQHFSEWANEALAGEDGESASGYWREQAAVAAESPLALADDLGEGEWTARRLLPRALLERLAANGLPEAAALLAWTQVAGQFQGDEGLPLEMARLVSGRLFNEFAELAGPFAGVAPLCLENVRAGSVGERLDALQAAILAQEEAAALRDPFAPDWPLAELGFAWLAGELDGAGVAELDCRQPPLGGFLELQVLPHGEGRLASLRVRRDHDGTLAGRLLDAWVECLESIAADRQLPLAGLPLIGAAERERYQAWQGERVEPAPVESLVAAFDLRAALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVERMREAGGIVFALADAECAGRAREAFAGACLDLSTLPLAGSGMSLPAPGGRDAAYMIFTSGTSGQPKGVVVEHASALNLSQALARTVYANVVGEGLRVTVNAPFSFDSSIKQILQLLSGHCLVLVPQEVRSDPQRMLGFLEERRIDVLDCTPSLFRLLLQAGLDDAHPALPGRILVGGERFDEASWEVAAGWRRCQVFNLYGPTEATVNASLARVAEHARPTIGRALANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVEEGWPGSGRLYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVLTDEADAAEPGADRRIVAFVTAAEETADESWLEVDLPSGHRVAGLNLNETEYVYQEIFVDEVYSRDGIVLPPDAVVLDVGANIGLFSLYIASRAPRARVVAFEPLAPIRRRLEANLGRYAPQVEVFGIGLSDAEREETFTYYPGYSTFSGIAEYADASGERDVIRRYLSNQGEEGGANLLLDNIDEILDDRLRAEAHRCRLRRLDQVIGELGLERIDLLKIDVQRAEMDVLLGLDDAALAKVRQIVLEVHDKRDGATAGRADALSDLLRRHGFEVSIRQDALLEGTDRYNCYAVRPGYAESLAERIDWRALAPRPAAALGGELSEQALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDRRALLAALAAEAAAQTLEAPANATEAALLEIWKSVLKRPAIGVSDNFFQVGGDSIRLIQMQVMAREAGLAFTLRDVFNHQSIRELARLLAAPASPADALGTSAPQSLEPFALLSAAERKRLPEGLDDAYPMTSLQQGMLLQSEASGDPRLLHNVVLHEVHGRLDGELLARAWAILIGRHAILRTGFDLHGGQVPLQWVHPATAVAAEVPVHDLCGLDGETRRLRLRAWIEEEQATPFDWSRPPLVRLAALALDERRFALGVAEHHSVLDGWSLQSLVDELLAVYADLLAGVVAREAEAPAVGFRDYVALEREAEANAASALFWLDYLAGARYRPLPGLAEEGPRRMAAVRVDVPADSLSRLRALAERSGLPLRSLLLAAHGRALCRFSDADEVVTGFVSHGRPEEPGADRLLGLFLNTLPCRLSASVDLLDSARRAFDYERASLEHRRHPLAAIRRRNRELRLDSLFNFVDFHQDDAAPAGVRHGGILDQVVVDVDVPLAVDFEVAGERLEVGFQYAAGRFPAERAEALAGAYREALLALLGDPVQPPAAAQAEDSVELRRVLKVLSRVLGRPLAADQGFASAGGHSLLGVQAIAELRRLTGRQLSLGLLQGDPDAREVVRRCHAADAPPLPPATERARALWLQRSGSAQPRLRLIALPPAGGNAGTFRGWDARLPADVELLAIQYPGRQERQDEPFVTDVEAMLCAIDDALLPLLDRPFALIGASLGGMLAYELAARLESLHGLRARQLFVISSRAPGPDLEYPRFHAMGDAELLRTLREYDVLPLEVLDDPELREISLATLRADSRLAADYRYRPREPLAIPITAILGEQDPGVSRVAIDGWRRHASRYELETLAGGHGLVVTAAEEVCAILRQRLAPDVPGGVPANLAT

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

6.2.1.68

Gene Ontology (GO)

GO:0016405 Catalysis of the reaction: substrate + ATP + CoASH = AMP + diphosphate + substrate-CoA.
GO:0031177 Binding to phosphopantetheine, the vitamin pantetheine 4'-(dihydrogen phosphate).
GO:0006631 The chemical reactions and pathways involving fatty acids, aliphatic monocarboxylic acids liberated from naturally occurring fats and oils by hydrolysis.
GO:0044550 The chemical reactions and pathways resulting in the formation of secondary metabolites, the compounds that are not necessarily required for growth and maintenance of cells, and are often unique to a taxon.
GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
GO:0009058 A cellular process consisting of the biochemical pathways by which a living organism synthesizes chemical substances. This typically represents the energy-requiring part of metabolism in which simpler substances are transformed into more complex ones.

Sequence Features

Domain/signature hits from InterPro and related databases.

65 records

Show feature table

Start	End	DB	Term	Name
593	604	ProSitePatterns	PS00455	Putative AMP-binding domain signature.
593	604	InterPro	IPR020845	AMP-binding, conserved site
1359	1780	Pfam	PF00668	Condensation domain
1359	1780	InterPro	IPR001242	Condensation domain
1355	1561	SUPERFAMILY	SSF52777	CoA-dependent acyltransferases
52	1641	PANTHER	PTHR43767	LONG-CHAIN-FATTY-ACID--COA LIGASE
1781	1860	Gene3D	G3DSA:1.10.1200.10	-
1781	1860	InterPro	IPR036736	ACP-like superfamily
1241	1326	Gene3D	G3DSA:1.10.1200.10	-
1241	1326	InterPro	IPR036736	ACP-like superfamily
203	438	Gene3D	G3DSA:3.30.559.30	Nonribosomal peptide synthetase, condensation domain
1360	1776	CDD	cd19536	DCL_NRPS-like
448	841	Gene3D	G3DSA:3.40.50.12780	-
448	841	InterPro	IPR042099	ANL, N-terminal domain
1791	1842	SMART	SM00823	Phosphopantetheine attachment site
1791	1842	InterPro	IPR020806	Polyketide synthase, phosphopantetheine-binding domain
1257	1325	SMART	SM00823	Phosphopantetheine attachment site
1257	1325	InterPro	IPR020806	Polyketide synthase, phosphopantetheine-binding domain
1248	1323	FunFam	G3DSA:1.10.1200.10:FF:000005	Nonribosomal peptide synthetase 1
1259	1321	Pfam	PF00550	Phosphopantetheine attachment site
1259	1321	InterPro	IPR009081	Phosphopantetheine binding ACP domain
1793	1854	Pfam	PF00550	Phosphopantetheine attachment site
1793	1854	InterPro	IPR009081	Phosphopantetheine binding ACP domain
414	1269	SUPERFAMILY	SSF56801	Acetyl-CoA synthetase-like
1888	2110	SMART	SM00824	Thioesterase
1888	2110	InterPro	IPR020802	Polyketide synthase, thioesterase domain
930	1153	Gene3D	G3DSA:3.40.50.150	Vaccinia Virus protein VP39
930	1153	InterPro	IPR029063	S-adenosyl-L-methionine-dependent methyltransferase superfamily
1814	1829	ProSitePatterns	PS00012	Phosphopantetheine attachment site.
1814	1829	InterPro	IPR006162	Phosphopantetheine attachment site
456	847	Pfam	PF00501	AMP-binding enzyme
456	847	InterPro	IPR000873	AMP-dependent synthetase/ligase domain
201	418	SUPERFAMILY	SSF52777	CoA-dependent acyltransferases
1250	1321	SUPERFAMILY	SSF47336	ACP-like
1250	1321	InterPro	IPR036736	ACP-like superfamily
1873	2111	Gene3D	G3DSA:3.40.50.1820	alpha/beta hydrolase
1873	2111	InterPro	IPR029058	Alpha/Beta hydrolase fold
1873	2110	SUPERFAMILY	SSF53474	alpha/beta-Hydrolases
1873	2110	InterPro	IPR029058	Alpha/Beta hydrolase fold
1553	1780	Gene3D	G3DSA:3.30.559.30	Nonribosomal peptide synthetase, condensation domain
17	202	Gene3D	G3DSA:3.30.559.10	-
17	202	InterPro	IPR023213	Chloramphenicol acetyltransferase-like domain superfamily
462	910	CDD	cd05930	A_NRPS
1886	2107	Pfam	PF00975	Thioesterase domain
1886	2107	InterPro	IPR001031	Thioesterase
1251	1325	ProSiteProfiles	PS50075	Carrier protein (CP) domain profile.
1251	1325	InterPro	IPR009081	Phosphopantetheine binding ACP domain
947	1122	NCBIfam	TIGR01444	FkbM family methyltransferase
947	1122	InterPro	IPR006342	Methyltransferase FkbM
1158	1239	Gene3D	G3DSA:3.30.300.30	-
1158	1239	InterPro	IPR045851	AMP-binding enzyme, C-terminal domain superfamily
950	1147	Pfam	PF05050	Methyltransferase FkbM domain
950	1147	InterPro	IPR006342	Methyltransferase FkbM
917	1152	SUPERFAMILY	SSF53335	S-adenosyl-L-methionine-dependent methyltransferases
917	1152	InterPro	IPR029063	S-adenosyl-L-methionine-dependent methyltransferase superfamily
1791	1853	SUPERFAMILY	SSF47336	ACP-like
1791	1853	InterPro	IPR036736	ACP-like superfamily
842	922	Gene3D	G3DSA:3.30.300.30	-
842	922	InterPro	IPR045851	AMP-binding enzyme, C-terminal domain superfamily
21	192	SUPERFAMILY	SSF52777	CoA-dependent acyltransferases
477	872	NCBIfam	TIGR01733	amino acid adenylation domain
477	872	InterPro	IPR010071	Amino acid adenylation domain
1354	1552	Gene3D	G3DSA:3.30.559.10	-
1354	1552	InterPro	IPR023213	Chloramphenicol acetyltransferase-like domain superfamily
1550	1778	SUPERFAMILY	SSF52777	CoA-dependent acyltransferases

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

1 + 1

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

Entry	Method	Resolution	Chain	Coverage	Links	Status
PDB 7R9X	X-ray	2.14 Å	A,B	20.5% 1353-1787	PDBe RCSB PDBj File	Viewing
AlphaFold PA2302	AlphaFold	—	—	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				0.871
3				0.421
2				0.315

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	42.2	0.968
2	6.98	0.361
3	0.99	0.005

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
4				0.553
2				0.339

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.

57 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
5FQ	5DUA	Q9Z4X6	158.2 Da LogP 0.64 TPSA 55.1	✓ Ro5	✓ Clean	`CCCCCNC(=O)[C@H](C)N`
CO8	7C1R	E5ATN9	893.7 Da LogP 1.03 TPSA 363.6	3 viol.	✓ Clean	`CCCCCCCC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)CO[P…`
FGU	7C1S	E5ATN9	232.3 Da LogP 0.76 TPSA 72.2	✓ Ro5	✓ Clean	`CC(C)C[C@@H](C(=O)SCCNC(=O)C)N`
FLC	6P1J	A0A0B5H0S3	189.1 Da LogP -5.25 TPSA 140.6	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O`
KH4	4PWV	F2YRY5	452.4 Da LogP -0.60 TPSA 190.9	1 viol.	✓ Clean	`CC(C)(COP(=O)(O)O)[C@H](C(=O)NCCC(=O)NCCSC(=O)c…`
SRP	6EA3	Q47NS0	434.3 Da LogP -2.99 TPSA 238.4	2 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
UM2	5DU9	Q9Z4X6	144.2 Da LogP 0.25 TPSA 55.1	✓ Ro5	✓ Clean	`CCCCNC(=O)[C@H](C)N`

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
ZINC31475423	1.000	434.3 Da LogP -2.99 TPSA 238.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@@](=O)(O)OC(=O)…`
ZINC106191477	0.958	200.3 Da LogP 1.81 TPSA 55.1	✓ Ro5	✓ Clean	`CCCCCCCCNC(=O)[C@H](C)N`
ZINC31516918	0.820	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…`
ZINC31539924	0.797	494.4 Da LogP -0.74 TPSA 218.2	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OC(=O…`
ZINC12360002	0.763	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	0.763	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	0.763	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	0.763	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	0.763	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	0.763	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	0.763	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586019	0.763	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	0.763	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586021	0.763	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	0.763	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC13518964	0.754	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC1532515	0.754	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	0.754	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC1842158	0.754	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	0.754	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC2126310	0.754	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3201891	0.754	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC3201893	0.754	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3830180	0.754	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3860156	0.754	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3977897	0.754	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	0.754	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	0.754	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	0.741	346.2 Da LogP -1.90 TPSA 191.9	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](N)(=O)O)[C@@…`
ZINC12503850	0.738	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	0.738	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	0.738	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	0.738	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	0.724	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	0.724	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	0.724	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC204538551	0.724	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC105469665	0.705	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	0.705	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	0.705	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	0.705	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	0.705	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	0.705	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	0.705	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@](=O)(O)CP(=O…`
ZINC106262372	0.690	256.4 Da LogP 3.23 TPSA 55.1	✓ Ro5	✓ Clean	`CCCCCCCCCCNC(=O)[C@@H](N)C(C)C`
ZINC147153902	0.690	284.5 Da LogP 4.01 TPSA 55.1	✓ Ro5	✓ Clean	`CCCCCCCCCCCCNC(=O)[C@@H](N)C(C)C`
ZINC5615251	0.689	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	0.689	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	0.689	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	0.689	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…`

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.