Protein profile

KP13_01965

Carbamoyl-phosphate synthase small chain

Genome: KpKP13

Gene: carA AHE46404.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GI28

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Amino acids 391

Annotations 8

Features 35

PDB binders 14

Druggability 0.232

Overview

Basic information about this protein and its source genome.

Accession: KP13_01965
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: carA AHE46404.1
Status: annotated
Amino acids: 391
Structure source: AlphaFold + ColabFold

6.3.5.5

GO:0004088 Catalysis of the reaction: hydrogencarbonate + L-glutamine + 2 ATP + H2O = carbamoyl phosphate + L-glutamate + 2 ADP + phosphate + 2 H+. 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:0006541 The chemical reactions and pathways involving glutamine, 2-amino-4-carbamoylbutanoic acid. GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0004359 Catalysis of the reaction: L-glutamine + H2O = L-glutamate + NH4+. 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 (%): 38.743
Human E-value: 1.3199999999999998e-68
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 72.296
DEG E-value: 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 96.64

Selected Druggability evidence

AlphaFold / UniProt model

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 0.232

Structure A0A0H3GI28

Pocket Pocket 5

P2Rank 0.601

Structure A0A0H3GI28

Pocket Pocket 1

ColabFold model

FPocket 0.381 · Pocket 5

P2Rank 0.684 · Pocket 1

Core conservation Accessory gene

Roary core

CoreCruncher accessory

Gut microbiome 248 / 4744 genomes with a hit

Normalized 0.052

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Enzyme Commission (EC)

6.3.5.5

Gene Ontology (GO)

GO:0004088 Catalysis of the reaction: hydrogencarbonate + L-glutamine + 2 ATP + H2O = carbamoyl phosphate + L-glutamate + 2 ADP + phosphate + 2 H+.
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:0006541 The chemical reactions and pathways involving glutamine, 2-amino-4-carbamoylbutanoic acid.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0004359 Catalysis of the reaction: L-glutamine + H2O = L-glutamate + NH4+.
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: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
245	254	PRINTS	PR00096	Glutamine amidotransferase superfamily signature
358	371	PRINTS	PR00096	Glutamine amidotransferase superfamily signature
273	284	PRINTS	PR00096	Glutamine amidotransferase superfamily signature
203	380	CDD	cd01744	GATase1_CPSase
203	380	InterPro	IPR035686	Carbamoyl-phosphate synthase small subunit, GATase1 domain
12	153	SUPERFAMILY	SSF52021	Carbamoyl phosphate synthetase, small subunit N-terminal domain
12	153	InterPro	IPR036480	Carbamoyl-phosphate synthase small subunit, N-terminal domain superfamily
12	142	SMART	SM01097	CPSase_sm_chain_2
12	142	InterPro	IPR002474	Carbamoyl-phosphate synthase small subunit, N-terminal domain
242	256	PRINTS	PR00099	Carbamoyl-phosphate synthase protein GATase domain signature
203	217	PRINTS	PR00099	Carbamoyl-phosphate synthase protein GATase domain signature
273	289	PRINTS	PR00099	Carbamoyl-phosphate synthase protein GATase domain signature
315	326	PRINTS	PR00099	Carbamoyl-phosphate synthase protein GATase domain signature
290	307	PRINTS	PR00099	Carbamoyl-phosphate synthase protein GATase domain signature
206	381	Pfam	PF00117	Glutamine amidotransferase class-I
206	381	InterPro	IPR017926	Glutamine amidotransferase
161	387	Gene3D	G3DSA:3.40.50.880	-
161	387	InterPro	IPR029062	Class I glutamine amidotransferase-like
12	368	PANTHER	PTHR11405	CARBAMOYLTRANSFERASE FAMILY MEMBER
14	384	NCBIfam	TIGR01368	glutamine-hydrolyzing carbamoyl-phosphate synthase small subunit
14	384	InterPro	IPR006274	Carbamoyl-phosphate synthase, small subunit
11	160	FunFam	G3DSA:3.50.30.20:FF:000001	Carbamoyl-phosphate synthase small chain
162	383	SUPERFAMILY	SSF52317	Class I glutamine amidotransferase-like
162	383	InterPro	IPR029062	Class I glutamine amidotransferase-like
161	388	FunFam	G3DSA:3.40.50.880:FF:000011	Carbamoyl-phosphate synthase small chain
12	387	Hamap	MF_01209	Carbamoyl-phosphate synthase small chain [carA].
12	387	InterPro	IPR006274	Carbamoyl-phosphate synthase, small subunit
11	160	Gene3D	G3DSA:3.50.30.20	-
11	160	InterPro	IPR036480	Carbamoyl-phosphate synthase small subunit, N-terminal domain superfamily
202	389	ProSiteProfiles	PS51273	Glutamine amidotransferase type 1 domain profile.
16	141	Pfam	PF00988	Carbamoyl-phosphate synthase small chain, CPSase domain
16	141	InterPro	IPR002474	Carbamoyl-phosphate synthase small subunit, N-terminal domain
245	254	PRINTS	PR00097	Anthranilate synthase component II signature
358	371	PRINTS	PR00097	Anthranilate synthase component II signature
273	284	PRINTS	PR00097	Anthranilate synthase component II signature

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 + 2

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

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold AF_A0A0H3GI28	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_01965	ColabFold	—	—	full sequence	—	Loaded

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				0.232

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Score	Probability
1	6.71	0.341
2	4.36	0.182
3	3.8	0.147
4	3.64	0.137
5	3.37	0.12

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				0.381

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Score	Probability
1	8.69	0.465
2	7.12	0.369
3	6.11	0.303
4	4.92	0.222
5	2.83	0.088

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.