Protein profile

PA4226

dihydroaeruginoic acid synthetase

Genome: NC_002516.2

Gene: pchE PA4226 Structure source: AlphaFold UniProt G3XCV2

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Amino acids 1438

Annotations 7

Features 50

PDB binders 6

Druggability 0.684

Overview

Basic information about this protein and its source genome.

Accession: PA4226
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: pchE PA4226
Status: annotated
Amino acids: 1438
Structure source: AlphaFold

6.2.1.69

GO:0016874 Catalysis of the joining of two molecules, or two groups within a single molecule, using the energy from the hydrolysis of ATP, a similar triphosphate, or a pH gradient. GO:0031177 Binding to phosphopantetheine, the vitamin pantetheine 4'-(dihydrogen phosphate). GO:0017000 The chemical reactions and pathways resulting in the formation of an antibiotic, a substance produced by or derived from certain fungi, bacteria, and other organisms, that can destroy or inhibit the growth of other microorganisms. GO:0072330 The chemical reactions and pathways resulting in the formation of monocarboxylic acids, any organic acid containing one carboxyl (-COOH) group. 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.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 39.08
Human E-value: 6.11e-08
Gut microbiome off-target: hit
Essential (DEG): N
Localization: Unknown

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 0.684

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MDLPPDSRTALRDWLTEQLADLLGEPLADVRALADDDDLLGCGLDSIRLMYLQERLRARGSTLDFAQLAQRPCLGAWLDLLACADRLSAPATVALPTAQDRDQPFELSSVQQAYWLGRGAGEVLGNVSCHAFLEFRTRDVDPQRLAAAAECVRQRHPMLRARFLDGRQQILPTPPLSCFDLQDWRTLQVDEAERDWQALRDWRAHECLAVERGQVFLLGLVRMPGGEDRLWLSLDLLAADVESLRLLLAELGVAYLAPERLAEPPALHFADYLAHRAAQRAEAAARARDYWLERLPRLPDAPALPLACAPESIRQPRTRRLAFQLSAGESRRLERLAAQHGVTLSSVFGCAFALVLARWSESAEFLLNVPLFDRHADDPRIGEVIADFTTLLLLECRMQAGVSFAEAVKSFQRNLHGAIDHAAFPALEVLREARRQGQPRSAPVVFASNLGEEGFVPAAFRDAFGDLHDMLSQTPQVWLDHQLYRVGDGILLAWDSVVGLFPEGLPETMFEAYVGLLQRLCDSAWGQPADLPLPWAQQARRALLNGQPACATARTLHRDFFLRAAEAPDADALLYRDQRVTRGELAERALRIAGGLREAGVRPGDAVEVSLPRGPQQVAAVFGVLAAGACYVPLDIDQPPARRRLIEEAAGVCLAITEEDDPQALPPRLDVQRLLRGPALAAPVPLAPQASAYVIYTSGSTGVPKGVEVSHAAAINTIDALLDLLRVNASDRLLAVSALDFDLSVFDLFGGLGAGASLVLPAQEQARDAAAWAEAIQRHAVSLWNSAPALLEMALSLPASQADYRSLRAVLLSGDWVALDLPGRLRPRCAEGCRLHVLGGATEAGIWSNLQSVDTVPPHWRSIPYGRPLPGQAYRVVDTHGRDVPDLVVGELWIGGASLARGYRNDPELSARRFVHDAQGRWYRTGDRGRYWGDGTLEFLGRVDQQVKVRGQRIELGEVEAALCAQAGVESACAAVLGGGVASLGAVLVPRLAPRAEGSMDLPAAQPFAGLAEAEAVLTREILGALLEAPLELDDGLRRRWLDWLADSAASALPSLDEALRRLGWQAAGLTAMGNALRGLLAGEQAPAALLLDPWLAPQAVAARLPDGREALARLLEALPTPAAGERLRVAVLDTRAGLWLDQGMASLLRPGLELTLFERSRVLLDAAATRLPERIVVQALDDGLLPAEHLGRYDRVISFAALHAYEASREGLALAAALLRPQGRLLLVDLLCESPLALLGAALLDDRPLRLAELPSLLADLAAAGLAPRCLWRSERIALVEALAPGLGLDAAALQAGLEQRLPQAMRPERLWCLPSLPLNGNGKVDRRRLAESMTRALGECRHEPSAEEPLEAHEQALAECWEAVLKRPVRRREASFFSLGGDSLLATRLLAGIRERFGVRLGMADFYRQPTLAGLARHLQVQTVEIEETQLEEGVL

MDLPPDSRTALRDWLTEQLADLLGEPLADVRALADDDDLLGCGLDSIRLMYLQERLRARGSTLDFAQLAQRPCLGAWLDLLACADRLSAPATVALPTAQDRDQPFELSSVQQAYWLGRGAGEVLGNVSCHAFLEFRTRDVDPQRLAAAAECVRQRHPMLRARFLDGRQQILPTPPLSCFDLQDWRTLQVDEAERDWQALRDWRAHECLAVERGQVFLLGLVRMPGGEDRLWLSLDLLAADVESLRLLLAELGVAYLAPERLAEPPALHFADYLAHRAAQRAEAAARARDYWLERLPRLPDAPALPLACAPESIRQPRTRRLAFQLSAGESRRLERLAAQHGVTLSSVFGCAFALVLARWSESAEFLLNVPLFDRHADDPRIGEVIADFTTLLLLECRMQAGVSFAEAVKSFQRNLHGAIDHAAFPALEVLREARRQGQPRSAPVVFASNLGEEGFVPAAFRDAFGDLHDMLSQTPQVWLDHQLYRVGDGILLAWDSVVGLFPEGLPETMFEAYVGLLQRLCDSAWGQPADLPLPWAQQARRALLNGQPACATARTLHRDFFLRAAEAPDADALLYRDQRVTRGELAERALRIAGGLREAGVRPGDAVEVSLPRGPQQVAAVFGVLAAGACYVPLDIDQPPARRRLIEEAAGVCLAITEEDDPQALPPRLDVQRLLRGPALAAPVPLAPQASAYVIYTSGSTGVPKGVEVSHAAAINTIDALLDLLRVNASDRLLAVSALDFDLSVFDLFGGLGAGASLVLPAQEQARDAAAWAEAIQRHAVSLWNSAPALLEMALSLPASQADYRSLRAVLLSGDWVALDLPGRLRPRCAEGCRLHVLGGATEAGIWSNLQSVDTVPPHWRSIPYGRPLPGQAYRVVDTHGRDVPDLVVGELWIGGASLARGYRNDPELSARRFVHDAQGRWYRTGDRGRYWGDGTLEFLGRVDQQVKVRGQRIELGEVEAALCAQAGVESACAAVLGGGVASLGAVLVPRLAPRAEGSMDLPAAQPFAGLAEAEAVLTREILGALLEAPLELDDGLRRRWLDWLADSAASALPSLDEALRRLGWQAAGLTAMGNALRGLLAGEQAPAALLLDPWLAPQAVAARLPDGREALARLLEALPTPAAGERLRVAVLDTRAGLWLDQGMASLLRPGLELTLFERSRVLLDAAATRLPERIVVQALDDGLLPAEHLGRYDRVISFAALHAYEASREGLALAAALLRPQGRLLLVDLLCESPLALLGAALLDDRPLRLAELPSLLADLAAAGLAPRCLWRSERIALVEALAPGLGLDAAALQAGLEQRLPQAMRPERLWCLPSLPLNGNGKVDRRRLAESMTRALGECRHEPSAEEPLEAHEQALAECWEAVLKRPVRRREASFFSLGGDSLLATRLLAGIRERFGVRLGMADFYRQPTLAGLARHLQVQTVEIEETQLEEGVL

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

6.2.1.69

Gene Ontology (GO)

GO:0016874 Catalysis of the joining of two molecules, or two groups within a single molecule, using the energy from the hydrolysis of ATP, a similar triphosphate, or a pH gradient.
GO:0031177 Binding to phosphopantetheine, the vitamin pantetheine 4'-(dihydrogen phosphate).
GO:0017000 The chemical reactions and pathways resulting in the formation of an antibiotic, a substance produced by or derived from certain fungi, bacteria, and other organisms, that can destroy or inhibit the growth of other microorganisms.
GO:0072330 The chemical reactions and pathways resulting in the formation of monocarboxylic acids, any organic acid containing one carboxyl (-COOH) group.
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.

Sequence Features

Domain/signature hits from InterPro and related databases.

50 records

Show feature table

Start	End	DB	Term	Name
136	442	Pfam	PF00668	Condensation domain
136	442	InterPro	IPR001242	Condensation domain
1350	1425	ProSiteProfiles	PS50075	Carrier protein (CP) domain profile.
1350	1425	InterPro	IPR009081	Phosphopantetheine binding ACP domain
8	86	FunFam	G3DSA:1.10.1200.10:FF:000021	Isochorismatase
1109	1268	SUPERFAMILY	SSF53335	S-adenosyl-L-methionine-dependent methyltransferases
1109	1268	InterPro	IPR029063	S-adenosyl-L-methionine-dependent methyltransferase superfamily
285	526	SUPERFAMILY	SSF52777	CoA-dependent acyltransferases
1342	1429	Gene3D	G3DSA:1.10.1200.10	-
1342	1429	InterPro	IPR036736	ACP-like superfamily
583	973	NCBIfam	TIGR01733	amino acid adenylation domain
583	973	InterPro	IPR010071	Amino acid adenylation domain
98	278	Gene3D	G3DSA:3.30.559.10	-
98	278	InterPro	IPR023213	Chloramphenicol acetyltransferase-like domain superfamily
283	525	FunFam	G3DSA:3.30.559.30:FF:000006	Yersiniabactin polyketide/non-ribosomal peptide synthetase
1380	1395	ProSitePatterns	PS00012	Phosphopantetheine attachment site.
1380	1395	InterPro	IPR006162	Phosphopantetheine attachment site
5	84	Gene3D	G3DSA:1.10.1200.10	-
5	84	InterPro	IPR036736	ACP-like superfamily
1349	1421	SUPERFAMILY	SSF47336	ACP-like
1349	1421	InterPro	IPR036736	ACP-like superfamily
1252	1341	Gene3D	G3DSA:3.30.300.30	-
1252	1341	InterPro	IPR045851	AMP-binding enzyme, C-terminal domain superfamily
1358	1421	Pfam	PF00550	Phosphopantetheine attachment site
1358	1421	InterPro	IPR009081	Phosphopantetheine binding ACP domain
13	80	Pfam	PF00550	Phosphopantetheine attachment site
13	80	InterPro	IPR009081	Phosphopantetheine binding ACP domain
99	276	FunFam	G3DSA:3.30.559.10:FF:000023	Non-ribosomal peptide synthetase
1344	1427	FunFam	G3DSA:1.10.1200.10:FF:000016	Non-ribosomal peptide synthase
332	1432	PANTHER	PTHR45527	NONRIBOSOMAL PEPTIDE SYNTHETASE
1142	1244	Gene3D	G3DSA:3.40.50.150	Vaccinia Virus protein VP39
1142	1244	InterPro	IPR029063	S-adenosyl-L-methionine-dependent methyltransferase superfamily
554	943	FunFam	G3DSA:3.40.50.12780:FF:000012	Non-ribosomal peptide synthetase
100	296	SUPERFAMILY	SSF52777	CoA-dependent acyltransferases
563	950	Pfam	PF00501	AMP-binding enzyme
563	950	InterPro	IPR000873	AMP-dependent synthetase/ligase domain
944	1054	Gene3D	G3DSA:3.30.300.30	-
944	1054	InterPro	IPR045851	AMP-binding enzyme, C-terminal domain superfamily
694	705	ProSitePatterns	PS00455	Putative AMP-binding domain signature.
694	705	InterPro	IPR020845	AMP-binding, conserved site
282	525	Gene3D	G3DSA:3.30.559.30	Nonribosomal peptide synthetase, condensation domain
6	117	SUPERFAMILY	SSF47336	ACP-like
6	117	InterPro	IPR036736	ACP-like superfamily
553	943	Gene3D	G3DSA:3.40.50.12780	-
553	943	InterPro	IPR042099	ANL, N-terminal domain
568	1042	CDD	cd12114	A_NRPS_TlmIV_like
104	523	CDD	cd19535	Cyc_NRPS
1356	1425	SMART	SM00823	Phosphopantetheine attachment site
1356	1425	InterPro	IPR020806	Polyketide synthase, phosphopantetheine-binding domain
543	1333	SUPERFAMILY	SSF56801	Acetyl-CoA synthetase-like

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 + 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 PA4226	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				0.582
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
AKR	6LTA	A0A077JG85	72.1 Da LogP 0.26 TPSA 37.3	✓ Ro5	✓ Clean	`C=CC(=O)O`
ANP	6LTB	A0A077JG85	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)…`
B6G	5WMM	Q333U7	432.3 Da LogP -1.37 TPSA 218.2	1 viol.	✓ Clean	`CC(C)[C@@H](C(=O)OP(=O)(O)O[C@H]1[C@H]([C@H]([C…`
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`
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)…`

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).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
5CA	A0A2S9PH42	7.40	449.5 Da LogP -3.34 TPSA 217.8	2 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`

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)…`
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…`
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…`
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(=…`
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…`
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…`
ZINC1582675	0.677	403.3 Da LogP 0.23 TPSA 164.1	1 viol.	✓ Clean	`CCOP(=O)(OCC)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[…`
ZINC5486730	0.677	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	0.677	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.