Protein target profile

KP13_02854

Putrescine aminotransferase

Genome: KpKP13 Gene: patA AHE42577.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GXV4

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Length 459

Pocket druggability 0.485

Direct ligand evidence 0 67 total records

Functional annotation 2 EC 8 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.

Main supporting evidence

Moderate predicted binding pocket FPocket selected-pocket score 0.48. This supports review but is not experimental validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.65. Structure available AlphaFold DB model + ColabFold model Ligand evidence via structure/bioactivity 13 structural and 4 bioactivity records.

Risks to review

Evidence gaps

No metabolic context No SBML/network-derived reaction evidence is loaded for 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
Human identity (%): 33.333 Lower values reduce human off-target concern.
Human E-value: 2.25e-61
Gut microbiome similarity: 1.6% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 0.0 Higher values support similarity to known essential genes.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 97.87 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

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 0.485

Structure A0A0H3GXV4

Pocket Pocket 6

P2Rank 0.651

Structure A0A0H3GXV4

Pocket Pocket 1

ColabFold model

FPocket 0.378 · Pocket 4

P2Rank 0.421 · Pocket 1

Core conservation Accessory gene

Roary core

CoreCruncher accessory

Gut microbiome 77 / 4744 genomes with a hit

Prevalence 1.6%

Cross-references

External database identifiers for this protein, its structures, ligands, and metabolic reactions.

Sequence

UniProt A0A0H3GXV4

Chemistry

ChEMBL CHEMBL1232972 ChEMBL CHEMBL220453 ChEMBL CHEMBL258218 ChEMBL CHEMBL330129

Sequence

Primary amino-acid sequence viewer.

MNRLPSSASALACSAHALNLIEKRTLDHEEMKALNQEVREYFKEHVNPGFLEYRKSVTAGGDYGAVEWQAGGLNTLVDTQGQEFIDCLGGFGIFNVGHRNPVVVSAVENQLAKQPLHSQELLDPLRAMLAKTLAALTPGKLKYSFFCNSGTESVEAALKLAKAYQSPRGKFTFIATSGAFHGKSLGALSATAKSTFRKPFMPLLPGFRHVPFGDITAMRTMLSECKKTGDDVAAVILEPIQGEGGVILPPTGYLPAVRKLCDEFGALLILDEVQTGMGRTGKMFACEHENVQPDILCLAKALGGGVMPIGATVATEEVFSVLFDNPFLHTTTFGGNPLACAAALATINVLLTQNLPAQAAQKGDMLLDGFRLLAQEYPDLVNEVRGKGMLMAIEFVDNEIGYDFASEMFRQRVLVAGTLNNAKTIRIEPPLTLTLEQCEQVLKAARKALAALRVSVEEA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

2 EC 8 GO

Enzyme Commission (EC)

Gene Ontology (GO)

GO:0030170 Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6.
GO:0008483 Catalysis of the transfer of an amino group to an acceptor, usually a 2-oxo acid.
GO:0009447 The chemical reactions and pathways resulting in the breakdown of putrescine, 1,4-diaminobutane; putrescine is the metabolic precursor of spermidine and spermine.
GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
GO:0033094 Catalysis of the reaction: putrescine + 2-oxoglutarate = L-glutamate + 1-pyrroline + H2O. The enzymatic part of the reaction produces 4-aminobutanal that spontaneously cyclizes to form 1-pyrroline.
GO:0019161 Catalysis of the reaction: an alpha,omega-diamine + 2-oxoglutarate = an omega-aminoaldehyde + L-glutamate.
GO:0042802 Binding to an identical protein or proteins.
GO:0019477 The chemical reactions and pathways resulting in the breakdown of L-lysine.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

28 records

Show feature table

Start	End	DB	Term	Name
4	12	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
35	447	Gene3D	G3DSA:3.90.1150.10	Aspartate Aminotransferase, domain 1
35	447	InterPro	IPR015422	Pyridoxal phosphate-dependent transferase, small domain
1	459	Hamap	MF_01276	Putrescine aminotransferase [patA].
1	459	InterPro	IPR017747	Putrescine aminotransferase
18	459	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
74	449	Pfam	PF00202	Aminotransferase class-III
74	449	InterPro	IPR005814	Aminotransferase class-III
100	353	FunFam	G3DSA:3.40.640.10:FF:000004	Acetylornithine aminotransferase
13	17	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
1	3	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
8	449	NCBIfam	TIGR03372	putrescine aminotransferase
8	449	InterPro	IPR017747	Putrescine aminotransferase
435	455	Coils	Coil	Coil
74	450	SUPERFAMILY	SSF53383	PLP-dependent transferases
74	450	InterPro	IPR015424	Pyridoxal phosphate-dependent transferase
100	353	Gene3D	G3DSA:3.40.640.10	-
100	353	InterPro	IPR015421	Pyridoxal phosphate-dependent transferase, major domain
268	305	ProSitePatterns	PS00600	Aminotransferases class-III pyridoxal-phosphate attachment site.
268	305	InterPro	IPR005814	Aminotransferase class-III
62	451	PANTHER	PTHR11986	AMINOTRANSFERASE CLASS III
52	209	PIRSF	PIRSF000521	Transaminase_4ab_Lys_Orn
52	209	InterPro	IPR005814	Aminotransferase class-III
213	452	PIRSF	PIRSF000521	Transaminase_4ab_Lys_Orn
213	452	InterPro	IPR005814	Aminotransferase class-III
74	440	CDD	cd00610	OAT_like
74	440	InterPro	IPR005814	Aminotransferase class-III
1	17	Phobius	SIGNAL_PEPTIDE	Signal peptide region

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.

'Alpha spheres' is FPocket's own cavity-shape geometry, imported when available and aligned with the loaded structure.

'Pocket atoms'/'Predicted site atoms' show the pocket's residue atoms instead: P2Rank reports residues rather than alpha spheres, and FPocket falls back to this when alpha-sphere geometry is unavailable or doesn't align.

'No pocket geometry' means neither alpha spheres nor residue-position data could be found for that pocket; the layer just highlights the same residues as 'Nearby residues'.

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 #6

0.485

Likely same site as P2Rank 2 1.1 Å 12 shared residues 100% of smaller site

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Surrounding area

Site 2 FPocket #4

0.332

Likely same site as P2Rank 4 2.2 Å 9 shared residues 100% of smaller site

Unusual size

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Surrounding area

Site 3 FPocket #7

0.329

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Surrounding area

Site 4 FPocket #11

0.244

Likely same site as P2Rank 1 7.7 Å 8 shared residues 89% of smaller site

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Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.651

Likely same site as FPocket 11 7.7 Å 8 shared residues 89% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.41

Likely same site as FPocket 6 1.1 Å 12 shared residues 100% of smaller site

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Surrounding area

Site 3 P2Rank #3

0.31

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Surrounding area

Site 4 P2Rank #4

0.152

Likely same site as FPocket 4 2.2 Å 9 shared residues 100% of smaller site

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Surrounding area

Site 5 P2Rank #5

0.059

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Surrounding area

Binding pockets · FPocket

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

Site 1 FPocket #4

0.378

Likely same site as P2Rank 3 1.7 Å 10 shared residues 83% of smaller site

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Surrounding area

Site 2 FPocket #20

0.355

Likely same site as P2Rank 1 2.6 Å 11 shared residues 100% of smaller site

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Surrounding area

Site 3 FPocket #17

0.346

Likely same site as P2Rank 2 1.2 Å 13 shared residues 100% of smaller site

Unusual size

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Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.421

Likely same site as FPocket 20 2.6 Å 11 shared residues 100% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.348

Likely same site as FPocket 17 1.2 Å 13 shared residues 100% of smaller site

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Surrounding area

Site 3 P2Rank #3

0.333

Likely same site as FPocket 4 1.7 Å 10 shared residues 83% of smaller site

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Surrounding area

Site 4 P2Rank #4

0.278

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Surrounding area

Site 5 P2Rank #5

0.173

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Surrounding area

All structural evidence 0 experimental · 2 predicted

Structural evidence

0 + 2

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
AlphaFold DB AF_A0A0H3GXV4	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_02854	ColabFold	—	—	full sequence	—	Loaded

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.

67 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 17 records from similar proteins

Structural ligands 13 0 loaded crystals

Measured bioactivity 4 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

9QJ PDB via homolog 358.3 Da · LogP 1.38 · TPSA 161.0 Open detail RCSB PDB

CAN PDB via homolog Detail RCSB PDB

GAB PDB via homolog Detail RCSB PDB

GBC PDB via homolog Detail RCSB PDB

IF1 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
9QJ RCSB PDB	5VWO	P04181	358.3 Da LogP 1.38 TPSA 161.0	✓ Ro5	✓ Clean	`[H]/N=C/1\C[C@H](C[C@H]1Cc2c(cnc(c2O)C)COP(=O)(…`
CAN RCSB PDB	2CAN	P04181	134.1 Da LogP -1.32 TPSA 98.6	✓ Ro5	✓ Clean	`C(CON)[C@@H](C(=O)O)N`
GAB RCSB PDB	1GBN	P04181	137.1 Da LogP 0.97 TPSA 63.3	✓ Ro5	✓ Clean	`c1cc(cc(c1)N)C(=O)O`
GBC RCSB PDB	1GBN	P04181	141.2 Da LogP 0.51 TPSA 63.3	✓ Ro5	✓ Clean	`C1CC(C=C(C1)C(=O)O)N`
IF1 RCSB PDB	7JX9	P04181	488.3 Da LogP 3.32 TPSA 149.5	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)/C=N/C2C[C@H](C[C@H]2C…`
MQ4 RCSB PDB	6OIA	P04181	237.2 Da LogP 1.07 TPSA 80.4	✓ Ro5	✓ Clean	`C1[C@@H](CC(=C1[C@@H](C=O)C(F)(F)F)N)C(=O)O`
PFM RCSB PDB	2OAT	P04181	374.3 Da LogP 0.96 TPSA 183.4	1 viol.	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)\C=C\C(=C\C[C@@H](C(=O…`
PMP RCSB PDB	6IO1	B9L0K9	248.2 Da LogP 0.16 TPSA 125.9	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CN)O`
POI RCSB PDB	1WKG	Q5SHH5	405.3 Da LogP 0.16 TPSA 178.3	1 viol.	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CNCCC[C@@H](C(=O)O)NC(…`
PPE RCSB PDB	1WKH	Q5SHH5	379.3 Da LogP -0.47 TPSA 187.8	1 viol.	✓ Clean	`Cc1c(c(c(c[nH+]1)COP(=O)(O)O)CN[C@@H](CCC(=O)O)…`
PUT RCSB PDB	4UOX	P42588	88.2 Da LogP -0.32 TPSA 52.0	✓ Ro5	✓ Clean	`C(CCN)CN`
VLS RCSB PDB	7JX9	P04181	179.2 Da LogP -2.62 TPSA 110.0	✓ Ro5	✓ Clean	`C(C(=O)O)NC(CO)(CO)CO`
Y3D RCSB PDB	7LK0	P04181	372.3 Da LogP 0.56 TPSA 166.6	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)/C=N/[C@H]2C[C@H](CC2=…`

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
CHEMBL1232972 ChEMBL	P04181	8.68 ~2.1 nM	141.2 Da LogP 0.51 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H]1C=C(C(=O)O)CCC1`
CHEMBL220453 ChEMBL	P04181	8.38 ~4.2 nM	277.2 Da LogP 2.23 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H]1C[C@@H](C(=O)O)CC1=C(C(F)(F)F)C(F)(F)F`
CHEMBL258218 ChEMBL	P04181	—	1050.0 Da LogP 8.07 TPSA 235.0	4 viol.	✓ Clean	`CC(CCCCNC(=O)CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@@H]2…`
CHEMBL330129 ChEMBL	P29758	—	127.1 Da LogP -0.19 TPSA 63.3	✓ Ro5	✓ Clean	`C#CC(N)CCC(=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
ZINC1685531 ZINC	0.875	200.4 Da LogP 2.80 TPSA 52.0	✓ Ro5	✓ Clean	`NCCCCCCCCCCCCN`
ZINC34273707 ZINC	0.875	256.5 Da LogP 4.37 TPSA 52.0	✓ Ro5	✓ Clean	`NCCCCCCCCCCCCCCCCN`
ZINC5178646 ZINC	0.875	228.4 Da LogP 3.59 TPSA 52.0	✓ Ro5	✓ Clean	`NCCCCCCCCCCCCCCN`
ZINC4245535 ZINC	0.769	213.2 Da LogP 2.63 TPSA 63.3	✓ Ro5	✓ Clean	`Nc1cccc(-c2cccc(C(=O)O)c2)c1`
ZINC156685 ZINC	0.708	212.3 Da LogP 2.08 TPSA 69.1	✓ Ro5	✓ Clean	`Nc1cccc(C(=O)c2cccc(N)c2)c1`
ZINC1532902 ZINC	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@@](O)(CC(=O)O)C(=O)O`
ZINC2018106 ZINC	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@](O)(CC(=O)O)C(=O)O`
ZINC12505568 ZINC	0.690	237.3 Da LogP 2.37 TPSA 63.3	✓ Ro5	✓ Clean	`Nc1cccc(C#Cc2cccc(C(=O)O)c2)c1`
ZINC34402619 ZINC	0.690	229.2 Da LogP 2.76 TPSA 72.5	✓ Ro5	✓ Clean	`Nc1cccc(Oc2cccc(C(=O)O)c2)c1`
ZINC486232 ZINC	0.677	256.3 Da LogP 2.22 TPSA 92.4	✓ Ro5	✓ Clean	`Nc1cccc(C(=O)Nc2cccc(C(=O)O)c2)c1`
ZINC521400454 ZINC	0.667	277.3 Da LogP 1.80 TPSA 97.5	✓ Ro5	✓ Clean	`Nc1cccc(S(=O)(=O)c2cccc(C(=O)O)c2)c1`
ZINC3593496 ZINC	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@@](O)(CC(=O)O)C(=O)O`
ZINC3593497 ZINC	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@](O)(CC(=O)O)C(=O)O`
ZINC1669765 ZINC	0.633	241.2 Da LogP 2.20 TPSA 80.4	✓ Ro5	✓ Clean	`Nc1cccc(C(=O)c2ccccc2C(=O)O)c1`
ZINC14686440 ZINC	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@](O)(CC(=O)NCCCCNC(=O)C[C@@](O)(CC(=O…`
ZINC14686442 ZINC	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@@](O)(CC(=O)NCCCCNC(=O)C[C@](O)(CC(=O…`
ZINC14686444 ZINC	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@@](O)(CC(=O)NCCCCNC(=O)C[C@@](O)(CC(=…`
ZINC4688104 ZINC	0.625	256.3 Da LogP 2.22 TPSA 92.4	✓ Ro5	✓ Clean	`Nc1cccc(C(=O)Nc2ccc(C(=O)O)cc2)c1`
ZINC2522309 ZINC	0.621	213.2 Da LogP 2.63 TPSA 63.3	✓ Ro5	✓ Clean	`Nc1ccc(-c2cccc(C(=O)O)c2)cc1`
ZINC2574116 ZINC	0.621	213.2 Da LogP 2.63 TPSA 63.3	✓ Ro5	✓ Clean	`Nc1cccc(-c2ccc(C(=O)O)cc2)c1`
ZINC207916 ZINC	0.600	270.2 Da LogP 2.31 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)c1cccc(C(=O)c2cccc(C(=O)O)c2)c1`
ZINC3897007 ZINC	0.600	242.2 Da LogP 2.75 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)c1cccc(-c2cccc(C(=O)O)c2)c1`
ZINC141320641 ZINC	0.581	203.2 Da LogP 2.40 TPSA 43.1	✓ Ro5	✓ Clean	`Nc1cccc(C(=O)CC(F)(F)F)c1`
ZINC291001 ZINC	0.581	212.3 Da LogP 2.52 TPSA 55.1	✓ Ro5	✓ Clean	`Nc1cccc(C(=O)Nc2ccccc2)c1`
ZINC71456252 ZINC	0.581	273.3 Da LogP 4.17 TPSA 43.1	✓ Ro5	✓ Clean	`Nc1cccc(C(=O)c2ccc(-c3ccccc3)cc2)c1`
ZINC13398039 ZINC	0.577	234.2 Da LogP -0.38 TPSA 121.1	✓ Ro5	✓ Clean	`CC(C)OC(=O)C[C@](O)(CC(=O)O)C(=O)O`
ZINC2528012 ZINC	0.577	234.2 Da LogP -0.38 TPSA 121.1	✓ Ro5	✓ Clean	`CC(C)OC(=O)C[C@@](O)(CC(=O)O)C(=O)O`
ZINC241850 ZINC	0.567	348.4 Da LogP 3.29 TPSA 104.6	✓ Ro5	✓ Clean	`Nc1cccc(C(=O)Oc2ccc(OC(=O)c3cccc(N)c3)cc2)c1`
ZINC619156 ZINC	0.567	346.4 Da LogP 3.36 TPSA 110.2	✓ Ro5	✓ Clean	`Nc1cccc(C(=O)Nc2ccc(NC(=O)c3cccc(N)c3)cc2)c1`
ZINC190579 ZINC	0.563	204.3 Da LogP 1.89 TPSA 46.3	✓ Ro5	✓ Clean	`Nc1cccc(C(=O)N2CCCCC2)c1`
ZINC7468685 ZINC	0.563	218.3 Da LogP 2.29 TPSA 46.3	✓ Ro5	✓ Clean	`Nc1cccc(C(=O)N2CCCCCC2)c1`
ZINC90600614 ZINC	0.563	229.2 Da LogP 2.76 TPSA 72.5	✓ Ro5	✓ Clean	`Nc1cccc(Oc2ccc(C(=O)O)cc2)c1`
ZINC95215251 ZINC	0.563	229.2 Da LogP 2.76 TPSA 72.5	✓ Ro5	Alert	`Nc1ccc(Oc2cccc(C(=O)O)c2)cc1`
ZINC146315135 ZINC	0.560	204.2 Da LogP 0.86 TPSA 94.8	✓ Ro5	✓ Clean	`CCCCC[C@@](O)(CC(=O)O)C(=O)O`
ZINC146315336 ZINC	0.560	204.2 Da LogP 0.86 TPSA 94.8	✓ Ro5	✓ Clean	`CCCCC[C@](O)(CC(=O)O)C(=O)O`
ZINC167226 ZINC	0.556	248.0 Da LogP 1.99 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)c1cccc(I)c1`
ZINC404749 ZINC	0.556	201.0 Da LogP 2.15 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)c1cccc(Br)c1`
ZINC409186 ZINC	0.556	226.2 Da LogP 2.62 TPSA 54.4	✓ Ro5	✓ Clean	`O=C(O)c1cccc(C(=O)c2ccccc2)c1`
ZINC1600851 ZINC	0.552	202.1 Da LogP 0.19 TPSA 94.8	✓ Ro5	✓ Clean	`O=C(O)c1cccc(P(=O)(O)O)c1`
ZINC65339755 ZINC	0.552	241.2 Da LogP 2.15 TPSA 80.4	✓ Ro5	✓ Clean	`NC(=O)c1cccc(-c2cccc(C(=O)O)c2)c1`
ZINC188631 ZINC	0.548	227.3 Da LogP 2.10 TPSA 81.1	✓ Ro5	✓ Clean	`Nc1cccc(NC(=O)c2cccc(N)c2)c1`
ZINC32012507 ZINC	0.548	211.3 Da LogP 2.81 TPSA 43.1	✓ Ro5	✓ Clean	`Cc1ccc(C(=O)c2cccc(N)c2)cc1`
ZINC32013043 ZINC	0.548	215.2 Da LogP 2.64 TPSA 43.1	✓ Ro5	✓ Clean	`Nc1cccc(C(=O)c2ccc(F)cc2)c1`
ZINC32016122 ZINC	0.548	231.7 Da LogP 3.15 TPSA 43.1	✓ Ro5	✓ Clean	`Nc1cccc(C(=O)c2ccc(Cl)cc2)c1`
ZINC32122261 ZINC	0.548	276.1 Da LogP 3.26 TPSA 43.1	✓ Ro5	✓ Clean	`Nc1cccc(C(=O)c2ccc(Br)cc2)c1`
ZINC75835494 ZINC	0.548	212.3 Da LogP 2.08 TPSA 69.1	✓ Ro5	Alert	`Nc1cccc(C(=O)c2ccccc2N)c1`
ZINC34552923 ZINC	0.545	227.3 Da LogP 2.63 TPSA 52.3	✓ Ro5	✓ Clean	`Nc1cccc(C(=O)OCc2ccccc2)c1`
ZINC41042309 ZINC	0.545	219.2 Da LogP 1.99 TPSA 52.3	✓ Ro5	✓ Clean	`Nc1cccc(C(=O)OCC(F)(F)F)c1`
ZINC96518109 ZINC	0.545	282.1 Da LogP 1.63 TPSA 77.2	✓ Ro5	✓ Clean	`CS(=O)(=O)C(Cl)(Cl)C(=O)c1cccc(N)c1`
ZINC96518468 ZINC	0.545	371.1 Da LogP 1.94 TPSA 77.2	✓ Ro5	✓ Clean	`CS(=O)(=O)C(Br)(Br)C(=O)c1cccc(N)c1`

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.