Protein profile

PA4756

carbamoyl phosphate synthase large subunit

Genome: NC_002516.2

Gene: PA4756 carB Structure source: AlphaFold UniProt P38100

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Amino acids 1073

Annotations 13

Features 80

PDB binders 14

Druggability 0.556

Overview

Basic information about this protein and its source genome.

Accession: PA4756
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA4756 carB
Status: annotated
Amino acids: 1073
Structure source: AlphaFold

6.3.4.16 6.3.5.5

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0004087 Catalysis of the reaction: 2 ATP + hydrogencarbonate + NH4+ = 2 ADP + carbamoyl phosphate + 2 H+ + phosphate. GO:0004088 Catalysis of the reaction: hydrogencarbonate + L-glutamine + 2 ATP + H2O = carbamoyl phosphate + L-glutamate + 2 ADP + phosphate + 2 H+. GO:0046872 Binding to a metal ion. GO:0044205 The chemical reactions and pathways resulting in the formation of UMP, uridine monophosphate, starting with the synthesis of (S)-dihydroorotate from bicarbonate; UMP biosynthesis may either occur via reduction by quinone, NAD+ or oxygen.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 43.958
Human E-value: 0.0
Gut microbiome off-target: hit
Essential (DEG): Y
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 0.556

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MPKRTDIKSILILGAGPIVIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPAMADATYIEPIKWATVAKIIEKERPDALLPTMGGQTALNCALDLERHGVLEKFGVEMIGANADTIDKAEDRSRFDKAMKDIGLACPRSGIAHSMEEAYGVLEQVGFPCIIRPSFTMGGTGGGIAYNREEFEEICARGLDLSPTNELLIDESLIGWKEYEMEVVRDKKDNCIIVCSIENFDPMGVHTGDSITVAPAQTLTDKEYQIMRNASLAVLREIGVETGGSNVQFGICPNTGRMVVIEMNPRVSRSSALASKATGFPIAKIAAKLAVGYTLDELQNDITGGRTPASFEPAIDYVVTKIPRFAFEKFPKADARLTTQMKSVGEVMAIGRTFQESVQKALRGLEVGATGFDPKLDLNDPEADSILKRELTVPSAERVWYVADAFRAGKSVEEVFELTRIDEWFLVQIEDLVKDEEKVKTLGLSSIDRELMYKLKRKGFSDARLAKLLGVTEKNLRSHRHKLKVLPVYKRVDTCAAEFATDTAYMYSTYEEECEANPSSREKIMILGGGPNRIGQGIEFDYCCVHAALAMREDGYETIMVNCNPETVSTDYDTSDRLYFEPVTLEDVLEIVRVEQPKGVIVQYGGQTPLKLCRALEEAGVPIIGTSPDAIDRAEDRERFQQMVQRLNLRQPANATARSEDEALAASKAIGYPLVVRPSYVLGGRAMEIVYQEEELKRYMREAVQVSNDSPVLLDHFLNCAIEVDIDAVCDGEIVVIGAIMQHIEQAGVHSGDSACSLPPYSLPQHIQDEIREQVKKMALELGVVGLMNVQMAVQGEDIFVIEVNPRASRTVPFVSKCVGESLAKVAARVMAGKTLAEVGFTQEIIPPFFSVKEAVFPFAKFPGVDPILGPEMKSTGEVMGVGDSFAEAFAKAQLGASEILPTAGCAFISVREDDKPFAAQVAGDLVALGFEVVATAGTARVIEAAGLPVRRVNKVTEGRPHVVDMIKNDEVTLIINTTEGRQSIADSYSIRRNALQHKICCTTTIAGGQAICEALKFGPEKTVRRLQDLHAGIKA

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

2 EC 11 GO

Enzyme Commission (EC)

Gene Ontology (GO)

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0004087 Catalysis of the reaction: 2 ATP + hydrogencarbonate + NH4+ = 2 ADP + carbamoyl phosphate + 2 H+ + phosphate.
GO:0004088 Catalysis of the reaction: hydrogencarbonate + L-glutamine + 2 ATP + H2O = carbamoyl phosphate + L-glutamate + 2 ADP + phosphate + 2 H+.
GO:0046872 Binding to a metal ion.
GO:0044205 The chemical reactions and pathways resulting in the formation of UMP, uridine monophosphate, starting with the synthesis of (S)-dihydroorotate from bicarbonate; UMP biosynthesis may either occur via reduction by quinone, NAD+ or oxygen.
GO:0071230 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an amino acid stimulus. An amino acid is a carboxylic acids containing one or more amino groups.
GO:0006536 The chemical reactions and pathways involving glutamate, the anion of 2-aminopentanedioic acid.
GO:0006541 The chemical reactions and pathways involving glutamine, 2-amino-4-carbamoylbutanoic acid.
GO:0006526 The chemical reactions and pathways resulting in the formation of arginine, 2-amino-5-(carbamimidamido)pentanoic acid.
GO:0006807 OBSOLETE. The chemical reactions and pathways involving organic or inorganic compounds that contain nitrogen.

Sequence Features

Domain/signature hits from InterPro and related databases.

80 records

Show feature table

Start	End	DB	Term	Name
6	1061	PANTHER	PTHR11405	CARBAMOYLTRANSFERASE FAMILY MEMBER
678	869	ProSiteProfiles	PS50975	ATP-grasp fold profile.
678	869	InterPro	IPR011761	ATP-grasp fold
936	1072	FunFam	G3DSA:3.40.50.1380:FF:000004	Carbamoyl-phosphate synthase large chain
405	553	FunFam	G3DSA:1.10.1030.10:FF:000002	Carbamoyl-phosphate synthase large chain
424	547	SMART	SM01096	CPSase_L_D3_2
424	547	InterPro	IPR005480	Carbamoyl-phosphate synthetase, large subunit oligomerisation domain
673	875	Pfam	PF02786	Carbamoyl-phosphate synthase L chain, ATP binding domain
673	875	InterPro	IPR005479	Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain
128	334	Pfam	PF02786	Carbamoyl-phosphate synthase L chain, ATP binding domain
128	334	InterPro	IPR005479	Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain
22	1073	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
955	1041	SMART	SM00851	MGS_2a
955	1041	InterPro	IPR011607	Methylglyoxal synthase-like domain
1	8	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
942	1051	CDD	cd01424	MGS_CPS_II
942	1051	InterPro	IPR033937	Carbamoyl-phosphate synthase large chain, methylglyoxal synthase-like domain
554	662	FunFam	G3DSA:3.40.50.20:FF:000003	Carbamoyl-phosphate synthase large chain
1	21	Phobius	SIGNAL_PEPTIDE	Signal peptide region
239	256	PRINTS	PR00098	Carbamoyl-phosphate synthase protein CPSase domain signature
239	256	InterPro	IPR005483	Carbamoyl-phosphate synthase large subunit, CPSase domain
48	58	PRINTS	PR00098	Carbamoyl-phosphate synthase protein CPSase domain signature
48	58	InterPro	IPR005483	Carbamoyl-phosphate synthase large subunit, CPSase domain
297	326	PRINTS	PR00098	Carbamoyl-phosphate synthase protein CPSase domain signature
297	326	InterPro	IPR005483	Carbamoyl-phosphate synthase large subunit, CPSase domain
204	223	PRINTS	PR00098	Carbamoyl-phosphate synthase protein CPSase domain signature
204	223	InterPro	IPR005483	Carbamoyl-phosphate synthase large subunit, CPSase domain
19	33	PRINTS	PR00098	Carbamoyl-phosphate synthase protein CPSase domain signature
19	33	InterPro	IPR005483	Carbamoyl-phosphate synthase large subunit, CPSase domain
380	398	PRINTS	PR00098	Carbamoyl-phosphate synthase protein CPSase domain signature
380	398	InterPro	IPR005483	Carbamoyl-phosphate synthase large subunit, CPSase domain
168	180	PRINTS	PR00098	Carbamoyl-phosphate synthase protein CPSase domain signature
168	180	InterPro	IPR005483	Carbamoyl-phosphate synthase large subunit, CPSase domain
119	403	FunFam	G3DSA:3.30.470.20:FF:000007	Carbamoyl-phosphate synthase large chain
554	662	Gene3D	G3DSA:3.40.50.20	-
838	845	ProSitePatterns	PS00867	Carbamoyl-phosphate synthase subdomain signature 2.
838	845	InterPro	IPR005479	Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain
404	553	Gene3D	G3DSA:1.10.1030.10	-
404	553	InterPro	IPR036897	Carbamoyl-phosphate synthetase, large subunit oligomerisation domain superfamily
665	935	FunFam	G3DSA:3.30.470.20:FF:000013	Carbamoyl-phosphate synthase large chain
119	403	Gene3D	G3DSA:3.30.470.20	-
1	116	FunFam	G3DSA:3.40.50.20:FF:000001	Carbamoyl-phosphate synthase large chain
427	505	Pfam	PF02787	Carbamoyl-phosphate synthetase large chain, oligomerisation domain
427	505	InterPro	IPR005480	Carbamoyl-phosphate synthetase, large subunit oligomerisation domain
1	116	Gene3D	G3DSA:3.40.50.20	-
938	1069	SUPERFAMILY	SSF52335	Methylglyoxal synthase-like
938	1069	InterPro	IPR036914	Methylglyoxal synthase-like domain superfamily
936	1072	Gene3D	G3DSA:3.40.50.1380	-
936	1072	InterPro	IPR036914	Methylglyoxal synthase-like domain superfamily
1	24	ProSiteProfiles	PS51257	Prokaryotic membrane lipoprotein lipid attachment site profile.
1	1062	Hamap	MF_01210_B	Carbamoyl-phosphate synthase large chain [carB].
1	1062	InterPro	IPR006275	Carbamoyl-phosphate synthase, large subunit
17	21	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
958	1041	Pfam	PF02142	MGS-like domain
958	1041	InterPro	IPR011607	Methylglyoxal synthase-like domain
709	723	ProSitePatterns	PS00866	Carbamoyl-phosphate synthase subdomain signature 1.
709	723	InterPro	IPR005479	Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain
686	755	FunFam	G3DSA:3.30.1490.20:FF:000001	Carbamoyl-phosphate synthase large chain
9	16	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
673	933	SUPERFAMILY	SSF56059	Glutathione synthetase ATP-binding domain-like
396	554	SUPERFAMILY	SSF48108	Carbamoyl phosphate synthetase, large subunit connection domain
396	554	InterPro	IPR036897	Carbamoyl-phosphate synthetase, large subunit oligomerisation domain superfamily
128	401	SUPERFAMILY	SSF56059	Glutathione synthetase ATP-binding domain-like
665	935	Gene3D	G3DSA:3.30.470.20	-
164	178	ProSitePatterns	PS00866	Carbamoyl-phosphate synthase subdomain signature 1.
164	178	InterPro	IPR005479	Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain
5	1067	Hamap	MF_01210_A	Carbamoyl-phosphate synthase large chain [carB].
5	1067	InterPro	IPR006275	Carbamoyl-phosphate synthase, large subunit
1	127	SUPERFAMILY	SSF52440	PreATP-grasp domain
1	127	InterPro	IPR016185	Pre-ATP-grasp domain superfamily
557	675	SUPERFAMILY	SSF52440	PreATP-grasp domain
557	675	InterPro	IPR016185	Pre-ATP-grasp domain superfamily
297	304	ProSitePatterns	PS00867	Carbamoyl-phosphate synthase subdomain signature 2.
297	304	InterPro	IPR005479	Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain
133	328	ProSiteProfiles	PS50975	ATP-grasp fold profile.
133	328	InterPro	IPR011761	ATP-grasp fold
2	1053	NCBIfam	TIGR01369	carbamoyl-phosphate synthase (glutamine-hydrolyzing) large subunit
2	1053	InterPro	IPR006275	Carbamoyl-phosphate synthase, large subunit
936	1073	ProSiteProfiles	PS51855	MGS-like domain profile.
936	1073	InterPro	IPR011607	Methylglyoxal synthase-like domain

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

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

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold PA4756	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				0.556
9				0.273
7				0.263

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.

87 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
0L1	4UTZ	P31327	146.1 Da LogP 0.72 TPSA 74.6	✓ Ro5	✓ Clean	`C(CCC(=O)O)CC(=O)O`
3NP	4UTX	P31327	119.1 Da LogP -0.26 TPSA 80.4	✓ Ro5	✓ Clean	`C(C[N+](=O)[O-])C(=O)O`
ANP	1BXR	P00968	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)…`
F9V	4UTV	P31327	194.2 Da LogP 1.33 TPSA 74.6	✓ Ro5	✓ Clean	`c1ccc(cc1)C(CC(=O)O)C(=O)O`
GUA	4UTR	P31327	132.1 Da LogP 0.33 TPSA 74.6	✓ Ro5	✓ Clean	`C(CC(=O)O)CC(=O)O`
IMP	1CE8	P00968	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)COP(=O)(O…`
JO3	4UU7	P31327	132.1 Da LogP 0.18 TPSA 74.6	✓ Ro5	✓ Clean	`CC(CC(=O)O)C(=O)O`
NLG	5DOU	P31327	189.2 Da LogP -0.56 TPSA 103.7	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](CCC(=O)O)C(=O)O`
NX6	4UUA	P31327	267.2 Da LogP 0.84 TPSA 112.9	✓ Ro5	✓ Clean	`c1ccc(cc1)COC(=O)N[C@@H](CC(=O)O)C(=O)O`
ORN	1CE8	P00968	132.2 Da LogP -0.86 TPSA 89.3	✓ Ro5	✓ Clean	`C(C[C@@H](C(=O)O)N)CN`
Q5A	6UEL	P31327	390.5 Da LogP 3.49 TPSA 65.5	✓ Ro5	✓ Clean	`Cc1csc(n1)NC(=O)C2CCN(CC2)C(=O)N(C)Cc3ccc(cc3)F`
SU8	4UUB	P31327	174.2 Da LogP 1.35 TPSA 74.6	✓ Ro5	✓ Clean	`CCCC[C@H](CC(=O)O)C(=O)O`
SUH	4UU7	P31327	132.1 Da LogP 0.18 TPSA 74.6	✓ Ro5	✓ Clean	`C[C@@H](CC(=O)O)C(=O)O`
WOC	4UU8	P31327	146.1 Da LogP 0.57 TPSA 74.6	✓ Ro5	✓ Clean	`CC(C)(CC(=O)O)C(=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`
CHEMBL4649653	P31327	7.18	409.5 Da LogP 3.69 TPSA 65.6	✓ Ro5	✓ Clean	`COc1ccc(C(=O)N2[C@H](C)CN(C(=O)c3ccc4cc[nH]c4c3…`
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`
CHEMBL4649844	P31327	6.89	432.5 Da LogP 3.75 TPSA 59.1	✓ Ro5	✓ Clean	`CCOc1ccc(C(=O)N2C[C@@H](C)N(C(=O)c3ccc(OC)cc3F)…`
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`
CHEMBL4638888	P31327	6.77	423.5 Da LogP 4.00 TPSA 65.6	✓ Ro5	✓ Clean	`COc1ccc(C(=O)N2[C@H](C)CN(C(=O)c3ccc4cc(C)[nH]c…`
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`
374	P31327	6.44	418.4 Da LogP 3.36 TPSA 59.1	✓ Ro5	✓ Clean	`C[C@@H]1CN(C[C@H](N1C(=O)c2ccc(cc2F)OC)C)C(=O)c…`
CHEMBL4634845	P31327	6.44	402.4 Da LogP 3.66 TPSA 49.9	✓ Ro5	✓ Clean	`COc1ccc(C(=O)N2C[C@@H](C)N(C(=O)c3ccc(C)cc3F)[C…`
CHEMBL4644019	P31327	6.42	432.5 Da LogP 3.75 TPSA 59.1	✓ Ro5	✓ Clean	`CCOc1ccc(C(=O)N2[C@H](C)CN(C(=O)c3ccc(OC)cc3F)C…`
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`
CHEMBL4634332	P31327	6.27	418.4 Da LogP 3.36 TPSA 59.1	✓ Ro5	✓ Clean	`COc1ccc(C(=O)N2[C@H](C)CN(C(=O)c3ccc(OC)c(F)c3)…`
CHEMBL1201780	P31327	—	190.2 Da LogP -1.03 TPSA 129.7	✓ Ro5	✓ Clean	`NC(=O)N[C@@H](CCC(=O)O)C(=O)O`

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
ZINC13862907	1.000	395.1 Da LogP 3.38 TPSA 90.7	✓ Ro5	✓ Clean	`Nc1ncc2cc(-c3c(Br)cccc3Br)c(N)nc2n1`
ZINC14951284	1.000	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C…`
ZINC1532551	1.000	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@…`
ZINC16969369	1.000	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@…`
ZINC1700285	1.000	267.2 Da LogP 0.84 TPSA 112.9	✓ Ro5	✓ Clean	`O=C(O)C[C@H](NC(=O)OCc1ccccc1)C(=O)O`
ZINC2004353	1.000	267.2 Da LogP 0.84 TPSA 112.9	✓ Ro5	✓ Clean	`O=C(O)C[C@@H](NC(=O)OCc1ccccc1)C(=O)O`
ZINC2382313256	1.000	390.5 Da LogP 3.49 TPSA 65.5	✓ Ro5	✓ Clean	`Cc1csc(NC(=O)C2CCN(C(=O)N(C)Cc3ccc(F)cc3)CC2)n1`
ZINC4228242	1.000	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@…`
ZINC4353761	1.000	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C…`
ZINC8614392	1.000	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C…`
ZINC1529497	0.917	230.3 Da LogP 3.06 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCC(=O)O`
ZINC1531045	0.917	202.2 Da LogP 2.28 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCC(=O)O`
ZINC1593115	0.917	216.3 Da LogP 2.67 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCC(=O)O`
ZINC1700020	0.917	244.3 Da LogP 3.45 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCC(=O)O`
ZINC3860440	0.917	258.4 Da LogP 3.84 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCC(=O)O`
ZINC3861298	0.917	286.4 Da LogP 4.62 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCCC(=O)O`
ZINC5113062	0.917	272.4 Da LogP 4.23 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCC(=O)O`
ZINC1689810	0.853	266.3 Da LogP 0.24 TPSA 118.7	✓ Ro5	✓ Clean	`NC(=O)C[C@H](NC(=O)OCc1ccccc1)C(=O)O`
ZINC1708468	0.853	357.4 Da LogP 2.50 TPSA 101.9	✓ Ro5	✓ Clean	`O=C(C[C@H](NC(=O)OCc1ccccc1)C(=O)O)OCc1ccccc1`
ZINC1845191	0.853	357.4 Da LogP 2.50 TPSA 101.9	✓ Ro5	✓ Clean	`O=C(C[C@@H](NC(=O)OCc1ccccc1)C(=O)O)OCc1ccccc1`
ZINC2022596	0.853	266.3 Da LogP 0.24 TPSA 118.7	✓ Ro5	✓ Clean	`NC(=O)C[C@@H](NC(=O)OCc1ccccc1)C(=O)O`
ZINC106686432	0.849	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP…`
ZINC12958393	0.849	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@@H](CO[P@](=O)(O)O…`
ZINC35024781	0.849	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)O…`
ZINC35024785	0.849	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)O…`
ZINC35024786	0.849	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)…`
ZINC4261903	0.849	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)O…`
ZINC80601236	0.849	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)O…`
ZINC95921560	0.849	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)O…`
ZINC170610434	0.844	418.4 Da LogP 3.36 TPSA 59.1	✓ Ro5	✓ Clean	`COc1ccc(C(=O)N2C[C@H](C)N(C(=O)c3ccc(OC)cc3F)[C…`
ZINC170610435	0.844	418.4 Da LogP 3.36 TPSA 59.1	✓ Ro5	✓ Clean	`COc1ccc(C(=O)N2C[C@H](C)N(C(=O)c3ccc(OC)cc3F)[C…`
ZINC170610436	0.844	418.4 Da LogP 3.36 TPSA 59.1	✓ Ro5	✓ Clean	`COc1ccc(C(=O)N2C[C@@H](C)N(C(=O)c3ccc(OC)cc3F)[…`
ZINC103601590	0.840	286.4 Da LogP 4.47 TPSA 74.6	✓ Ro5	✓ Clean	`CCCCCCCCCCCC[C@@H](CC(=O)O)C(=O)O`
ZINC103601597	0.840	286.4 Da LogP 4.47 TPSA 74.6	✓ Ro5	✓ Clean	`CCCCCCCCCCCC[C@H](CC(=O)O)C(=O)O`
ZINC1603111	0.840	258.4 Da LogP 3.69 TPSA 74.6	✓ Ro5	✓ Clean	`CCCCCCCCCC[C@H](CC(=O)O)C(=O)O`
ZINC2027042	0.840	258.4 Da LogP 3.69 TPSA 74.6	✓ Ro5	✓ Clean	`CCCCCCCCCC[C@@H](CC(=O)O)C(=O)O`
ZINC2566748	0.840	202.2 Da LogP 2.13 TPSA 74.6	✓ Ro5	✓ Clean	`CCCCCC[C@@H](CC(=O)O)C(=O)O`
ZINC3199210	0.840	202.2 Da LogP 2.13 TPSA 74.6	✓ Ro5	✓ Clean	`CCCCCC[C@H](CC(=O)O)C(=O)O`
ZINC1702215	0.824	357.4 Da LogP 2.50 TPSA 101.9	✓ Ro5	✓ Clean	`O=C(O)C[C@H](NC(=O)OCc1ccccc1)C(=O)OCc1ccccc1`
ZINC1744563	0.824	357.4 Da LogP 2.50 TPSA 101.9	✓ Ro5	✓ Clean	`O=C(O)C[C@@H](NC(=O)OCc1ccccc1)C(=O)OCc1ccccc1`
ZINC1532510	0.821	304.3 Da LogP -1.60 TPSA 170.1	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CCC(=O)O)C(=…`
ZINC1532511	0.821	304.3 Da LogP -1.60 TPSA 170.1	✓ Ro5	✓ Clean	`CC(=O)N[C@H](CC(=O)O)C(=O)N[C@@H](CCC(=O)O)C(=O…`
ZINC1532512	0.821	304.3 Da LogP -1.60 TPSA 170.1	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](CC(=O)O)C(=O)N[C@H](CCC(=O)O)C(=O…`
ZINC1532513	0.821	304.3 Da LogP -1.60 TPSA 170.1	✓ Ro5	✓ Clean	`CC(=O)N[C@H](CC(=O)O)C(=O)N[C@H](CCC(=O)O)C(=O)O`
ZINC66267769	0.821	372.5 Da LogP 3.35 TPSA 65.5	✓ Ro5	✓ Clean	`Cc1csc(NC(=O)C2CCN(C(=O)N(C)Cc3ccccc3)CC2)n1`
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…`
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(=…`
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(=…`

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.