Protein target profile

HT085_RS00270

glutamine-hydrolyzing carbamoyl-phosphate synthase small subunit

Genome: NZ_AP023069.1 Gene: TUM19854C_00450 carA 3D evidence: ColabFold model

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Length 377

Direct ligand evidence 0 71 total records

Functional annotation 0 EC 1 GO

Target summary

Target candidate with partial support; inspect missing evidence before prioritizing.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Terms and data sources used on this page

PDB: experimentally determined structures from the Protein Data Bank. These are the strongest structural evidence, but may cover only part of the protein.

AlphaFold DB model: a precomputed predicted structure downloaded from AlphaFold Database/UniProt, not an experiment performed here.

ColabFold model: a predicted structure generated for this workspace; interpret it with coverage and confidence.

pLDDT: confidence score for predicted structures. High values support local geometry; low values mean the region should not drive pocket interpretation.

FPocket / P2Rank: software tools that predict possible ligand-binding pockets on a 3D structure. They are useful screening signals, not experimental validation.

Druggability: a pocket-based estimate of whether a small molecule could bind productively. It does not mean a drug already exists.

PDB ligand: a compound observed in an experimental structure. Direct same-protein records are stronger than homolog-transferred records.

ChEMBL: a public database of measured compound bioactivity. Direct entries are stronger than entries transferred from similar proteins.

ZINC: a purchasable-compound database. Here it marks proposed candidates from chemical similarity, not measured binders.

LigQ / LigQ_2: an internal Target pipeline step that gathers PDB, ChEMBL, and ZINC ligand evidence for each protein.

Off-target: sequence similarity to proteins we prefer not to hit, such as human proteins or beneficial gut microbiome proteins.

DEG: Database of Essential Genes. A match suggests the protein resembles genes known to be essential in other organisms.

Roary / CoreCruncher: pan-genome tools used to decide whether a gene is core across analyzed strains or accessory/strain-specific.

EC / GO: functional annotations: EC describes enzyme reactions; GO describes biological process, molecular function, or cellular component.

KEGG pathway: a curated metabolic route label used here to group reactions imported from the metabolic model.

Chokepoint: a metabolic reaction that is the only producer or consumer of a metabolite in the imported model.

Prioritization evidence

Selectivity, essentiality, structural confidence, conservation, and predicted binding-site evidence.

Off-target risk

Human off-target: Hit
Gut microbiome off-target: Hit

Essentiality

Essential (DEG): Y

Localization

Localization: Cytoplasmic

Binding-site evidence

The selected pocket score is the FPocket value used for ranking after applying the curated structure priority. It estimates small-molecule pocket quality; it is not experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

FPocket Medium

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MSTPALLVLADGSVFHGTSIGYEGSASGEVVFNTSMTGYQEILTDPSYCKQIVTLTYPHIGNTGTNAEDEESRSVYAAGLIIRDLPLLHSSFRASESLHDYLVRNETVAIADIDTRRLTMLLREKGAQGGAILTGADATVEKAQELIAAFGSMVGKDLAKEVSCTETYEWTEGEWELGKGFVTPDKQPYHVVAYDFGVKTNILRMLASRGCRLTVVPAQTSAEDVLALNPDGVFLSNGPGDPEPCTYAIEAVQKLMESGKPIFGICLGHQLISLAIGAKTLKMRFSHHGANHPVQDLDSGKVVITSQNHGFAVDADTLPANARITHKSLFDNTLQGIELTDKPVFCFQGHPEASPGPQDVGYLFDKFIGNMKAAKQA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 GO

Gene Ontology (GO)

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.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

32 records

Show feature table

Start	End	DB	Term	Name
4	141	SUPERFAMILY	SSF52021	Carbamoyl phosphate synthetase, small subunit N-terminal domain
4	141	InterPro	IPR036480	Carbamoyl-phosphate synthase small subunit, N-terminal domain superfamily
191	368	CDD	cd01744	GATase1_CPSase
191	368	InterPro	IPR035686	Carbamoyl-phosphate synthase small subunit, GATase1 domain
3	151	Gene3D	G3DSA:3.50.30.20	-
3	151	InterPro	IPR036480	Carbamoyl-phosphate synthase small subunit, N-terminal domain superfamily
152	376	FunFam	G3DSA:3.40.50.880:FF:000011	Carbamoyl-phosphate synthase small chain
5	356	PANTHER	PTHR11405	CARBAMOYLTRANSFERASE FAMILY MEMBER
346	359	PRINTS	PR00096	Glutamine amidotransferase superfamily signature
261	272	PRINTS	PR00096	Glutamine amidotransferase superfamily signature
233	242	PRINTS	PR00096	Glutamine amidotransferase superfamily signature
3	375	Hamap	MF_01209	Carbamoyl-phosphate synthase small chain [carA].
3	375	InterPro	IPR006274	Carbamoyl-phosphate synthase, small subunit
2	150	FunFam	G3DSA:3.50.30.20:FF:000001	Carbamoyl-phosphate synthase small chain
278	295	PRINTS	PR00099	Carbamoyl-phosphate synthase protein GATase domain signature
303	314	PRINTS	PR00099	Carbamoyl-phosphate synthase protein GATase domain signature
230	244	PRINTS	PR00099	Carbamoyl-phosphate synthase protein GATase domain signature
261	277	PRINTS	PR00099	Carbamoyl-phosphate synthase protein GATase domain signature
191	205	PRINTS	PR00099	Carbamoyl-phosphate synthase protein GATase domain signature
194	368	Pfam	PF00117	Glutamine amidotransferase class-I
194	368	InterPro	IPR017926	Glutamine amidotransferase
155	373	SUPERFAMILY	SSF52317	Class I glutamine amidotransferase-like
155	373	InterPro	IPR029062	Class I glutamine amidotransferase-like
5	372	NCBIfam	TIGR01368	glutamine-hydrolyzing carbamoyl-phosphate synthase small subunit
5	372	InterPro	IPR006274	Carbamoyl-phosphate synthase, small subunit
152	375	Gene3D	G3DSA:3.40.50.880	-
152	375	InterPro	IPR029062	Class I glutamine amidotransferase-like
190	377	ProSiteProfiles	PS51273	Glutamine amidotransferase type 1 domain profile.
3	133	SMART	SM01097	CPSase_sm_chain_2
3	133	InterPro	IPR002474	Carbamoyl-phosphate synthase small subunit, N-terminal domain
7	132	Pfam	PF00988	Carbamoyl-phosphate synthase small chain, CPSase domain
7	132	InterPro	IPR002474	Carbamoyl-phosphate synthase small subunit, N-terminal domain

3D structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; AlphaFold DB and ColabFold models typically cover the full protein but remain computational predictions.

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Pocket score High Medium Low

How colors and pocket overlays are used

Uniform protein color marks the displayed model as a single molecular object.

Experimental PDB structures may be colored by chain to distinguish subunits or copies present in the file.

Pocket colors and alpha spheres are evidence overlays for predicted binding cavities; they are not alternative protein chains.

Pocket details Inspect a specific pocket, or open the full viewer

Binding pockets · FPocket

Druggability: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Site 1 FPocket #1

0.636

Show in viewer

Surrounding area

All structural evidence 0 experimental · 1 predicted

Structural evidence

0 + 1

Experimental PDB entries plus predicted AlphaFold DB or ColabFold models. Click Switch to display a different loaded structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
ColabFold HT085_RS00270	ColabFold	—	—	full sequence	—	Viewing

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

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 21 records from similar proteins

Structural ligands 14 0 loaded crystals

Measured bioactivity 7 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

0L1 PDB via homolog 146.1 Da · LogP 0.72 · TPSA 74.6 Open detail RCSB PDB

374 PDB via homolog Detail RCSB PDB

3NP PDB via homolog Detail RCSB PDB

F9V PDB via homolog Detail RCSB PDB

GUA PDB via homolog Detail RCSB PDB

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in Target, 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 RCSB PDB	4UTZ	P31327	146.1 Da LogP 0.72 TPSA 74.6	✓ Ro5	✓ Clean	`C(CCC(=O)O)CC(=O)O`
374 RCSB PDB	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 RCSB PDB	4UTX	P31327	119.1 Da LogP -0.26 TPSA 80.4	✓ Ro5	✓ Clean	`C(C[N+](=O)[O-])C(=O)O`
F9V RCSB PDB	4UTV	P31327	194.2 Da LogP 1.33 TPSA 74.6	✓ Ro5	✓ Clean	`c1ccc(cc1)C(CC(=O)O)C(=O)O`
GUA RCSB PDB	4UTR	P31327	132.1 Da LogP 0.33 TPSA 74.6	✓ Ro5	✓ Clean	`C(CC(=O)O)CC(=O)O`
IMP RCSB PDB	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 RCSB PDB	4UU7	P31327	132.1 Da LogP 0.18 TPSA 74.6	✓ Ro5	✓ Clean	`CC(CC(=O)O)C(=O)O`
NLG RCSB PDB	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 RCSB PDB	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 RCSB PDB	1CE8	P0A6F1	132.2 Da LogP -0.86 TPSA 89.3	✓ Ro5	✓ Clean	`C(C[C@@H](C(=O)O)N)CN`
Q5A RCSB PDB	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 RCSB PDB	4UUB	P31327	174.2 Da LogP 1.35 TPSA 74.6	✓ Ro5	✓ Clean	`CCCC[C@H](CC(=O)O)C(=O)O`
SUH RCSB PDB	4UU7	P31327	132.1 Da LogP 0.18 TPSA 74.6	✓ Ro5	✓ Clean	`C[C@@H](CC(=O)O)C(=O)O`
WOC RCSB PDB	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 ChEMBL	P31327	7.18 ~66.1 nM	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 ChEMBL	P31327	6.89 ~128.8 nM	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 ChEMBL	P31327	6.77 ~169.8 nM	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 ChEMBL	P31327	6.44 ~363.1 nM	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 ChEMBL	P31327	6.42 ~380.2 nM	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 ChEMBL	P31327	6.27 ~537.0 nM	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 ChEMBL	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	0.917	230.3 Da LogP 3.06 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCC(=O)O`
ZINC1531045 ZINC	0.917	202.2 Da LogP 2.28 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCC(=O)O`
ZINC1593115 ZINC	0.917	216.3 Da LogP 2.67 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCC(=O)O`
ZINC1700020 ZINC	0.917	244.3 Da LogP 3.45 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCC(=O)O`
ZINC3860440 ZINC	0.917	258.4 Da LogP 3.84 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCC(=O)O`
ZINC3861298 ZINC	0.917	286.4 Da LogP 4.62 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCCC(=O)O`
ZINC5113062 ZINC	0.917	272.4 Da LogP 4.23 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCC(=O)O`
ZINC1689810 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	0.840	286.4 Da LogP 4.47 TPSA 74.6	✓ Ro5	✓ Clean	`CCCCCCCCCCCC[C@@H](CC(=O)O)C(=O)O`
ZINC103601597 ZINC	0.840	286.4 Da LogP 4.47 TPSA 74.6	✓ Ro5	✓ Clean	`CCCCCCCCCCCC[C@H](CC(=O)O)C(=O)O`
ZINC1603111 ZINC	0.840	258.4 Da LogP 3.69 TPSA 74.6	✓ Ro5	✓ Clean	`CCCCCCCCCC[C@H](CC(=O)O)C(=O)O`
ZINC2027042 ZINC	0.840	258.4 Da LogP 3.69 TPSA 74.6	✓ Ro5	✓ Clean	`CCCCCCCCCC[C@@H](CC(=O)O)C(=O)O`
ZINC2566748 ZINC	0.840	202.2 Da LogP 2.13 TPSA 74.6	✓ Ro5	✓ Clean	`CCCCCC[C@@H](CC(=O)O)C(=O)O`
ZINC3199210 ZINC	0.840	202.2 Da LogP 2.13 TPSA 74.6	✓ Ro5	✓ Clean	`CCCCCC[C@H](CC(=O)O)C(=O)O`
ZINC1702215 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	0.800	266.3 Da LogP 0.24 TPSA 118.7	✓ Ro5	✓ Clean	`NC(=O)[C@@H](CC(=O)O)NC(=O)OCc1ccccc1`
ZINC2030861 ZINC	0.800	266.3 Da LogP 0.24 TPSA 118.7	✓ Ro5	✓ Clean	`NC(=O)[C@H](CC(=O)O)NC(=O)OCc1ccccc1`
ZINC2560710 ZINC	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 ZINC	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.