Protein profile

PA1400

pyruvate carboxylase

Genome: NC_002516.2

Gene: PA1400 Structure source: AlphaFold UniProt Q9I3U4

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Amino acids 1095

Annotations 5

Features 43

PDB binders 9

Druggability 0.56

Overview

Basic information about this protein and its source genome.

Accession: PA1400
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA1400
Status: annotated
Amino acids: 1095
Structure source: AlphaFold

GO:0003989 Catalysis of the reaction: ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA. GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0046872 Binding to a metal ion. GO:0006633 The chemical reactions and pathways resulting in the formation of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes. 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.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 57.576
Human E-value: 2.44e-06
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 0.56

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MTAPFNALLIANRGEIAIRIARACADLGIRSVAVFAEDDAASLHVRKADVALPLAGRGVAAYLDMDRLVALALEQGCEAIHPGYGFLAENGEFARRCQRAGIHFVGPQAEVLDLFGDKAAARALAERLEVPLVAGINRAVSVEEAEAFLEGLGDGAAVMLKALAGGGGRGMRAVEEVAQLADAYRRCRAEAQAAFGRDELYVEQRVARARHIEVQVLGDGSGAVSHLWERDCSLQRRQQKLLEIAPSPDLPEATREALIDCALRMAGAVRYRGIGTFEFLVDDERPGRFYFMEANPRIQVEHTVTEEVTGVDLLHAQLRLAAGMELAALGLERPPAIGGCAVQLRINLETLAADGSARPAVGTIGAYEPPSGPGLRVDGYGYAGYRVSPSYDSLLAKLVVRGADYPAALRRAYRALCEFRLEGVASNLDLLRNLLLHPAVQANRVDTRFVESHLETLLAPIPASHPRLRAECPLAEDAAPARVEAPLGSLPLSAPSSGVLVALEVADGERVRAGQRVAILEAMKMEFEVKAPGGGIVRRLAASLGEPLEEGATLLFLEPTEDDDEQAPTEQALDLAHIRADLAEVLERQAALGDERRPQALARRRKTGQRTARENVLDLLDEGSFSEYGGFALAAQRRRRSAEELLELSPADGLVAGTGTVGAASFGVQAARCLVLAYDYTVFAGTQGVMNHKKTDRLLGLAEQWRLPLVLFAEGGGGRPGDTDFVGVAGLDCHTFVGMARLSGLVPLVGVVSGRCFAGNAALLGCCDVIIATRDATIGMAGPAMIEGGGLGRFAAEEVGPTGVQGPNGVIDVLVEDEAEAVAVARRYLGYFQGPLPDWSCADQRELRHLVPENRLRAYDIRQAIEVLADRGSVLELRRQFAPGLVTALLRIEGRAFGLIANNPGHLGGAIDAAAGDKAARFMQLCDAFDIPIVSLCDTPGFMVGPEAEKQATVRHVSRMFVSAASLTVPFFTVVLRKGYGLGAQAMAAGSFHSPLFTVAWPSGEFGAMGLEGAVRLGFAKELAAEEDPQRREALFRGMVDKAYRNGKALNMASYLEIDAVIDPAETRAWLLRGLAVAGEPAPRAGRKRPFVDTW

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

5 GO

Gene Ontology (GO)

GO:0003989 Catalysis of the reaction: ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0046872 Binding to a metal ion.
GO:0006633 The chemical reactions and pathways resulting in the formation of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes.
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.

Sequence Features

Domain/signature hits from InterPro and related databases.

43 records

Show feature table

Start	End	DB	Term	Name
122	322	ProSiteProfiles	PS50975	ATP-grasp fold profile.
122	322	InterPro	IPR011761	ATP-grasp fold
206	462	Gene3D	G3DSA:3.30.470.20	-
492	559	Gene3D	G3DSA:2.40.50.100	-
291	298	ProSitePatterns	PS00867	Carbamoyl-phosphate synthase subdomain signature 2.
291	298	InterPro	IPR005479	Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain
3	114	SUPERFAMILY	SSF52440	PreATP-grasp domain
3	114	InterPro	IPR016185	Pre-ATP-grasp domain superfamily
581	838	SUPERFAMILY	SSF52096	ClpP/crotonase
581	838	InterPro	IPR029045	ClpP/crotonase-like domain superfamily
343	451	Pfam	PF02785	Biotin carboxylase C-terminal domain
343	451	InterPro	IPR005482	Biotin carboxylase, C-terminal
338	457	SUPERFAMILY	SSF51246	Rudiment single hybrid motif
338	457	InterPro	IPR011054	Rudiment single hybrid motif
493	555	Pfam	PF00364	Biotin-requiring enzyme
493	555	InterPro	IPR000089	Biotin/lipoyl attachment
514	531	ProSitePatterns	PS00188	Biotin-requiring enzymes attachment site.
514	531	InterPro	IPR001882	Biotin-binding site
3	533	PANTHER	PTHR48095	PYRUVATE CARBOXYLASE SUBUNIT A
807	1075	SUPERFAMILY	SSF52096	ClpP/crotonase
807	1075	InterPro	IPR029045	ClpP/crotonase-like domain superfamily
117	327	Pfam	PF02786	Carbamoyl-phosphate synthase L chain, ATP binding domain
117	327	InterPro	IPR005479	Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain
5	112	Pfam	PF00289	Biotin carboxylase, N-terminal domain
5	112	InterPro	IPR005481	Biotin carboxylase-like, N-terminal domain
561	834	Gene3D	G3DSA:3.90.226.10	-
842	1095	ProSiteProfiles	PS50989	Acetyl-coenzyme A (CoA) carboxyltransferase C-terminal domain profile.
842	1095	InterPro	IPR011763	Acetyl-coenzyme A carboxyltransferase, C-terminal
842	1095	Gene3D	G3DSA:3.90.226.10	-
4	455	ProSiteProfiles	PS50979	Biotin carboxylation domain profile.
4	455	InterPro	IPR011764	Biotin carboxylation domain
343	451	SMART	SM00878	Biotin_carb_C_2
134	204	Gene3D	G3DSA:3.30.1490.20	-
134	204	InterPro	IPR013815	ATP-grasp fold, subdomain 1
492	557	CDD	cd06850	biotinyl_domain
605	1076	Pfam	PF01039	Carboxyl transferase domain
605	1076	InterPro	IPR034733	Acetyl-CoA carboxylase
486	558	SUPERFAMILY	SSF51230	Single hybrid motif
486	558	InterPro	IPR011053	Single hybrid motif
1	133	Gene3D	G3DSA:3.40.50.20	-
85	334	SUPERFAMILY	SSF56059	Glutathione synthetase ATP-binding domain-like
480	558	ProSiteProfiles	PS50968	Biotinyl/lipoyl domain profile.
480	558	InterPro	IPR000089	Biotin/lipoyl attachment

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 PA1400	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
5				0.302
1				0.285

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.

74 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
3PY	4MFE	Q2K340	104.1 Da LogP -1.37 TPSA 74.6	✓ Ro5	✓ Clean	`C(C(=O)C(=O)O)O`
AGS	2QF7	Q2K340	523.2 Da LogP -1.51 TPSA 262.1	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
BPV	4MIM	Q2K340	167.0 Da LogP 0.03 TPSA 54.4	✓ Ro5	✓ Clean	`C(C(=O)C(=O)O)Br`
BTI	3BG5	A0A0H3JRU9	228.3 Da LogP 0.91 TPSA 58.2	✓ Ro5	✓ Clean	`C1[C@H]2[C@@H]([C@@H](S1)CCCCC=O)NC(=O)N2`
BYT	4M6V	Q2K340	372.5 Da LogP 0.41 TPSA 133.6	✓ Ro5	✓ Clean	`C1[C@H]2[C@@H]([C@@H](S1)CCCCC(=O)NCCCC[C@@H](C…`
OXL	4MFD	Q2K340	88.0 Da LogP -3.51 TPSA 80.3	✓ Ro5	✓ Clean	`C(=O)(C(=O)[O-])[O-]`
PAE	3TW6	Q2K340	140.0 Da LogP -0.75 TPSA 94.8	✓ Ro5	✓ Clean	`C(C(=O)O)P(=O)(O)O`
PYR	4JX5	Q2K340	88.1 Da LogP -0.34 TPSA 54.4	✓ Ro5	✓ Clean	`CC(=O)C(=O)O`
TAR	4ISS	Q6CP22	150.1 Da LogP -2.12 TPSA 115.1	✓ Ro5	✓ Clean	`[C@H]([C@@H](C(=O)O)O)(C(=O)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).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
CHEMBL4466052	P37798	7.50	378.8 Da LogP 3.58 TPSA 112.8	✓ Ro5	✓ Clean	`COc1ccc(-c2cccc(Cl)c2-c2cc3cnc(N)nc3nc2N)cn1`
CHEMBL4518489	P37798	7.48	387.3 Da LogP 2.97 TPSA 94.0	✓ Ro5	✓ Clean	`Nc1ncc2cc(-c3c(Cl)cccc3Cl)c(N3C[C@@H]4[C@@H](N)…`
CHEMBL4530311	P37798	7.44	348.8 Da LogP 3.57 TPSA 103.6	✓ Ro5	✓ Clean	`Nc1ncc2cc(-c3c(Cl)cccc3-c3cccnc3)c(N)nc2n1`
CHEMBL4459017	P37798	7.19	389.3 Da LogP 3.37 TPSA 94.0	✓ Ro5	✓ Clean	`NCC1CCN(c2nc3nc(N)ncc3cc2-c2c(Cl)cccc2Cl)C1`
CHEMBL4450292	P37798	7.10	313.4 Da LogP 3.52 TPSA 90.7	✓ Ro5	✓ Clean	`Nc1ncc2cc(-c3ccccc3-c3ccccc3)c(N)nc2n1`
CHEMBL4563086	P37798	7.08	405.3 Da LogP 2.48 TPSA 114.2	✓ Ro5	✓ Clean	`NCC1(O)CCN(c2nc3nc(N)ncc3cc2-c2c(Cl)cccc2Cl)C1`
CHEMBL4445287	P37798	7.03	343.8 Da LogP 3.54 TPSA 99.9	✓ Ro5	✓ Clean	`CC(C)COc1cccc(Cl)c1-c1cc2cnc(N)nc2nc1N`
CHEMBL4551132	P37798	6.89	314.4 Da LogP 2.92 TPSA 103.6	✓ Ro5	✓ Clean	`Nc1ncc2cc(-c3ccccc3-c3cccnc3)c(N)nc2n1`
CHEMBL4564355	P37798	6.85	390.3 Da LogP 3.40 TPSA 88.2	✓ Ro5	✓ Clean	`Nc1ncc2cc(-c3c(Cl)cccc3Cl)c(N3CCC(CO)C3)nc2n1`
CHEMBL4582507	P37798	6.77	403.3 Da LogP 2.89 TPSA 111.0	✓ Ro5	✓ Clean	`NC(=O)C1CCN(c2nc3nc(N)ncc3cc2-c2c(Cl)cccc2Cl)C1`
CHEMBL57531	P37798	6.75	395.1 Da LogP 3.38 TPSA 90.7	✓ Ro5	✓ Clean	`Nc1ncc2cc(-c3c(Br)cccc3Br)c(N)nc2n1`
CHEMBL4440951	P37798	6.72	405.3 Da LogP 2.48 TPSA 114.2	✓ Ro5	✓ Clean	`Nc1ncc2cc(-c3c(Cl)cccc3Cl)c(N3CCC(N)(CO)C3)nc2n1`
CHEMBL4464608	P37798	6.50	403.3 Da LogP 3.76 TPSA 94.0	✓ Ro5	✓ Clean	`NCC1CCN(c2nc3nc(N)ncc3cc2-c2c(Cl)cccc2Cl)CC1`
CHEMBL58627	P37798	6.50	306.2 Da LogP 3.16 TPSA 90.7	✓ Ro5	✓ Clean	`Nc1ncc2cc(-c3c(Cl)cccc3Cl)c(N)nc2n1`
CHEMBL4520904	P37798	6.36	407.3 Da LogP 3.46 TPSA 94.0	✓ Ro5	✓ Clean	`NCC1(F)CCN(c2nc3nc(N)ncc3cc2-c2c(Cl)cccc2Cl)C1`

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
ZINC13542455	1.000	372.5 Da LogP 0.41 TPSA 133.5	✓ Ro5	✓ Clean	`N[C@H](CCCCNC(=O)CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@…`
ZINC13862907	1.000	395.1 Da LogP 3.38 TPSA 90.7	✓ Ro5	✓ Clean	`Nc1ncc2cc(-c3c(Br)cccc3Br)c(N)nc2n1`
ZINC4096827	1.000	372.5 Da LogP 0.41 TPSA 133.5	✓ Ro5	✓ Clean	`N[C@@H](CCCCNC(=O)CCCC[C@@H]1SC[C@@H]2NC(=O)N[C…`
ZINC71756253	1.000	372.5 Da LogP 0.41 TPSA 133.5	✓ Ro5	✓ Clean	`N[C@H](CCCCNC(=O)CCCC[C@H]1SC[C@H]2NC(=O)N[C@H]…`
ZINC71756255	1.000	372.5 Da LogP 0.41 TPSA 133.5	✓ Ro5	✓ Clean	`N[C@H](CCCCNC(=O)CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@…`
ZINC71756256	1.000	372.5 Da LogP 0.41 TPSA 133.5	✓ Ro5	✓ Clean	`N[C@H](CCCCNC(=O)CCCC[C@@H]1SC[C@H]2NC(=O)N[C@H…`
ZINC71756257	1.000	372.5 Da LogP 0.41 TPSA 133.5	✓ Ro5	✓ Clean	`N[C@H](CCCCNC(=O)CCCC[C@@H]1SC[C@H]2NC(=O)N[C@@…`
ZINC208820459	0.868	371.5 Da LogP 0.86 TPSA 140.3	1 viol.	✓ Clean	`N=C(O)[C@H](N)CCCCNC(=O)CCCC[C@@H]1SC[C@H]2NC(=…`
ZINC12360002	0.855	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	0.855	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	0.855	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	0.855	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	0.855	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	0.855	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	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586019	0.855	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	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586021	0.855	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	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC149461335	0.849	371.5 Da LogP -0.19 TPSA 139.3	✓ Ro5	✓ Clean	`NC(=O)[C@H](N)CCCCNC(=O)CCCC[C@@H]1SC[C@@H]2NC(…`
ZINC4899883	0.849	371.5 Da LogP -0.19 TPSA 139.3	✓ Ro5	✓ Clean	`NC(=O)[C@@H](N)CCCCNC(=O)CCCC[C@@H]1SC[C@@H]2NC…`
ZINC504704915	0.849	371.5 Da LogP -0.19 TPSA 139.3	✓ Ro5	✓ Clean	`NC(=O)[C@H](N)CCCCNC(=O)CCCC[C@@H]1SC[C@H]2NC(=…`
ZINC504704916	0.849	371.5 Da LogP -0.19 TPSA 139.3	✓ Ro5	✓ Clean	`NC(=O)[C@H](N)CCCCNC(=O)CCCC[C@@H]1SC[C@@H]2NC(…`
ZINC13518964	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC1532515	0.782	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	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC1842158	0.782	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	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC2126310	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3201891	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC3201893	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3830180	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3860156	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3977897	0.782	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	0.782	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	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC149304428	0.769	343.4 Da LogP 1.08 TPSA 107.5	✓ Ro5	✓ Clean	`O=C(O)CCCCNC(=O)CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@H…`
ZINC228146714	0.769	314.5 Da LogP 0.57 TPSA 96.2	✓ Ro5	✓ Clean	`NCCCCNC(=O)CCCC[C@H]1SC[C@@H]2NC(=O)N[C@H]21`
ZINC228146725	0.769	314.5 Da LogP 0.57 TPSA 96.2	✓ Ro5	✓ Clean	`NCCCCNC(=O)CCCC[C@H]1SC[C@H]2NC(=O)N[C@H]21`
ZINC95628810	0.769	314.5 Da LogP 0.57 TPSA 96.2	✓ Ro5	✓ Clean	`NCCCCNC(=O)CCCC[C@@H]1SC[C@H]2NC(=O)N[C@@H]21`
ZINC95628811	0.769	314.5 Da LogP 0.57 TPSA 96.2	✓ Ro5	✓ Clean	`NCCCCNC(=O)CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12`
ZINC4096224	0.768	346.2 Da LogP -1.90 TPSA 191.9	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](N)(=O)O)[C@@…`
ZINC12503850	0.763	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	0.763	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	0.763	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	0.763	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OS(=O…`
ZINC144798305	0.755	357.5 Da LogP 1.47 TPSA 107.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCNC(=O)CCCC[C@H]1SC[C@H]2NC(=O)N[C@H]…`
ZINC2069434709	0.755	379.9 Da LogP 4.71 TPSA 77.6	✓ Ro5	✓ Clean	`CSc1ncc2cc(-c3c(Cl)cccc3-c3cccnc3)c(N)nc2n1`
ZINC22051793	0.755	441.6 Da LogP 3.81 TPSA 107.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCNC(=O)CCCC[C@@H]1SC[C@H]2NC(=O…`
ZINC33759367	0.755	357.5 Da LogP 1.47 TPSA 107.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCNC(=O)CCCC[C@@H]1SC[C@H]2NC(=O)N[C@H…`

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.