Protein profile

PA4758

carbamoyl phosphate synthase small subunit

Genome: NC_002516.2

Gene: carA PA4758 Structure source: AlphaFold UniProt P38098

Export view

Amino acids 378

Annotations 11

Features 35

PDB binders 14

Druggability 0.498

Overview

Basic information about this protein and its source genome.

Accession: PA4758
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: carA PA4758
Status: annotated
Amino acids: 378
Structure source: AlphaFold

6.3.5.5

GO:0005951 A protein complex that catalyzes the formation of carbamoyl phosphate; comprises a small subunit that binds and cleaves glutamine, and a large subunit that accepts the ammonia group cleaved from glutamine, binds all of the remaining substrates and effectors, and carries out all of the other catalytic events. 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:0004088 Catalysis of the reaction: hydrogencarbonate + L-glutamine + 2 ATP + H2O = carbamoyl phosphate + L-glutamate + 2 ADP + phosphate + 2 H+. GO:0004359 Catalysis of the reaction: L-glutamine + H2O = L-glutamate + NH4+. GO:0006207 The chemical reactions and pathways resulting in the formation of pyrimidine nucleobases, 1,3-diazine, organic nitrogenous bases, beginning with the synthesis of a pyrimidine ring from simpler precursors.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 38.903
Human E-value: 5.3000000000000004e-67
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 0.498

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 10 GO

Enzyme Commission (EC)

6.3.5.5

Gene Ontology (GO)

GO:0005951 A protein complex that catalyzes the formation of carbamoyl phosphate; comprises a small subunit that binds and cleaves glutamine, and a large subunit that accepts the ammonia group cleaved from glutamine, binds all of the remaining substrates and effectors, and carries out all of the other catalytic events.
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:0004088 Catalysis of the reaction: hydrogencarbonate + L-glutamine + 2 ATP + H2O = carbamoyl phosphate + L-glutamate + 2 ADP + phosphate + 2 H+.
GO:0004359 Catalysis of the reaction: L-glutamine + H2O = L-glutamate + NH4+.
GO:0006207 The chemical reactions and pathways resulting in the formation of pyrimidine nucleobases, 1,3-diazine, organic nitrogenous bases, beginning with the synthesis of a pyrimidine ring from simpler precursors.
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: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.

Sequence Features

Domain/signature hits from InterPro and related databases.

35 records

Show feature table

Start	End	DB	Term	Name
2	151	Gene3D	G3DSA:3.50.30.20	-
2	151	InterPro	IPR036480	Carbamoyl-phosphate synthase small subunit, N-terminal domain superfamily
7	132	Pfam	PF00988	Carbamoyl-phosphate synthase small chain, CPSase domain
7	132	InterPro	IPR002474	Carbamoyl-phosphate synthase small subunit, N-terminal domain
5	375	NCBIfam	TIGR01368	glutamine-hydrolyzing carbamoyl-phosphate synthase small subunit
5	375	InterPro	IPR006274	Carbamoyl-phosphate synthase, small subunit
2	151	FunFam	G3DSA:3.50.30.20:FF:000001	Carbamoyl-phosphate synthase small chain
194	371	CDD	cd01744	GATase1_CPSase
194	371	InterPro	IPR035686	Carbamoyl-phosphate synthase small subunit, GATase1 domain
152	378	FunFam	G3DSA:3.40.50.880:FF:000011	Carbamoyl-phosphate synthase small chain
3	133	SMART	SM01097	CPSase_sm_chain_2
3	133	InterPro	IPR002474	Carbamoyl-phosphate synthase small subunit, N-terminal domain
197	372	Pfam	PF00117	Glutamine amidotransferase class-I
197	372	InterPro	IPR017926	Glutamine amidotransferase
4	144	SUPERFAMILY	SSF52021	Carbamoyl phosphate synthetase, small subunit N-terminal domain
4	144	InterPro	IPR036480	Carbamoyl-phosphate synthase small subunit, N-terminal domain superfamily
3	360	PANTHER	PTHR11405	CARBAMOYLTRANSFERASE FAMILY MEMBER
152	377	Gene3D	G3DSA:3.40.50.880	-
152	377	InterPro	IPR029062	Class I glutamine amidotransferase-like
236	245	PRINTS	PR00096	Glutamine amidotransferase superfamily signature
264	275	PRINTS	PR00096	Glutamine amidotransferase superfamily signature
349	362	PRINTS	PR00096	Glutamine amidotransferase superfamily signature
194	208	PRINTS	PR00099	Carbamoyl-phosphate synthase protein GATase domain signature
264	280	PRINTS	PR00099	Carbamoyl-phosphate synthase protein GATase domain signature
281	298	PRINTS	PR00099	Carbamoyl-phosphate synthase protein GATase domain signature
306	317	PRINTS	PR00099	Carbamoyl-phosphate synthase protein GATase domain signature
233	247	PRINTS	PR00099	Carbamoyl-phosphate synthase protein GATase domain signature
3	378	Hamap	MF_01209	Carbamoyl-phosphate synthase small chain [carA].
3	378	InterPro	IPR006274	Carbamoyl-phosphate synthase, small subunit
264	275	PRINTS	PR00097	Anthranilate synthase component II signature
349	362	PRINTS	PR00097	Anthranilate synthase component II signature
236	245	PRINTS	PR00097	Anthranilate synthase component II signature
193	378	ProSiteProfiles	PS51273	Glutamine amidotransferase type 1 domain profile.
153	377	SUPERFAMILY	SSF52317	Class I glutamine amidotransferase-like
153	377	InterPro	IPR029062	Class I glutamine amidotransferase-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...

Legend High Medium Low

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 PA4758	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
2				0.498
1				0.45

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.

71 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`
374	6W2J	P31327	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…`
3NP	4UTX	P31327	119.1 Da LogP -0.26 TPSA 80.4	✓ Ro5	✓ Clean	`C(C[N+](=O)[O-])C(=O)O`
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	P0A6F1	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	P0A6F1	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
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…`
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)…`
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…`
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…`
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
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`
ZINC107269764	0.806	265.3 Da LogP 1.35 TPSA 92.7	✓ Ro5	✓ Clean	`CC(=O)C[C@H](NC(=O)OCc1ccccc1)C(=O)O`
ZINC107269767	0.806	265.3 Da LogP 1.35 TPSA 92.7	✓ Ro5	✓ Clean	`CC(=O)C[C@@H](NC(=O)OCc1ccccc1)C(=O)O`
ZINC1558677	0.800	266.3 Da LogP 0.24 TPSA 118.7	✓ Ro5	✓ Clean	`NC(=O)[C@@H](CC(=O)O)NC(=O)OCc1ccccc1`
ZINC2030861	0.800	266.3 Da LogP 0.24 TPSA 118.7	✓ Ro5	✓ Clean	`NC(=O)[C@H](CC(=O)O)NC(=O)OCc1ccccc1`
ZINC2560710	0.800	372.4 Da LogP 2.29 TPSA 114.0	✓ Ro5	✓ Clean	`O=C(NC[C@H](NC(=O)OCc1ccccc1)C(=O)O)OCc1ccccc1`
ZINC39397035	0.800	372.4 Da LogP 2.29 TPSA 114.0	✓ Ro5	✓ Clean	`O=C(NC[C@@H](NC(=O)OCc1ccccc1)C(=O)O)OCc1ccccc1`

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.