Protein target profile

KP13_03835

Protein aegA

Genome: KpKP13 Gene: aegA AHE43319.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GWI5

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Length 660

Pocket druggability 0.937

Direct ligand evidence 0 58 total records

Functional annotation 0 EC 5 GO

Target summary

Promising target candidate with multiple supporting evidence streams.

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

Main supporting evidence

Independent pocket support: FPocket + P2Rank Both predictors report a high-scoring binding site (FPocket 0.94, P2Rank 0.93). Use the 3D pocket comparison to verify whether they identify the same site. Strong predicted binding pocket FPocket selected-pocket score 0.94. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.93. Structure available AlphaFold DB model + ColabFold model Review the complete evidence below

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 (%): 29.63 Lower values reduce human off-target concern.
Human E-value: 4.96e-08
Gut microbiome similarity: 1.5% 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: 93.26 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 0.937

Structure A0A0H3GWI5

Pocket Pocket 1

P2Rank 0.931

Structure A0A0H3GWI5

Pocket Pocket 1

ColabFold model

FPocket 0.957 · Pocket 1

P2Rank 0.944 · Pocket 1

Core conservation Accessory gene

Roary accessory

CoreCruncher accessory

Gut microbiome 72 / 4744 genomes with a hit

Prevalence 1.5%

Cross-references

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

Sequence

UniProt A0A0H3GWI5

Sequence

Primary amino-acid sequence viewer.

MNHFILSDSRKCIGCQACEVACVMAHNEEQHVLTPQRFLPRITVIKAEGQRNAITCRHCEDAPCVRSCPNDAIAQSGDSVQVRQEKCIGCKSCMVACPFGVMQVVVTPQAAGLVKASAHKCDLCQGREAGPACVENCPAQALTLADDETLITLAKQRRLRSACQEVQPWQRATPLCSQPNAGAKVRQMAMTPPRGEPDKLAAEVRKSHFEEIYQPFTPEQAQQQAARCLTCGEHSICEWTCPLHNHIPQWIELVKAGNIAAAVALSHQTNCLPEITGRVCPQDRLCEGACTLRDESGAVTIGNIERYISDQALASGWRPDLSQVKPSGKRVAIIGAGPAGLACADMLVRHGVQPVVFDRHPEIGGLLTFGIPAFKLDKSLLARRRAIFSEMGIRFELNCEVGKDISMATLLADYDAVFVGAGTYRSMKAGLPNEEAPGVYDALPFLIANTKQVMGLAASAQEPYVNTAGLNVVVLGGGDTAMDCVRTALRHGARQVTCAYRRDEANMPGSKKEVKNAREEGALFEFNVQPVTLELDENGRVNGVRFLRTELGAPDAGGRRRPTPIPGSEFVMPADAVIMAFGFHPHRMPWLEAAGVALDSQGRIKAGVESRYRYQTSQEKIFAGGDAVRGADLVVTAMAEGRHAAQGILDYLARKTTPLH

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

5 GO

Gene Ontology (GO)

GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
GO:0051539 Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands.
GO:0051536 Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms.
GO:0046872 Binding to a metal ion.
GO:0044281 The chemical reactions and pathways involving small molecules, any low molecular weight, monomeric, non-encoded molecule.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

35 records

Show feature table

Start	End	DB	Term	Name
189	652	NCBIfam	TIGR01318	glutamate synthase, small subunit
189	652	InterPro	IPR006006	Glutamate synthase NADPH small chain-like
114	147	ProSiteProfiles	PS51379	4Fe-4S ferredoxin-type iron-sulfur binding domain profile.
114	147	InterPro	IPR017896	4Fe-4S ferredoxin-type, iron-sulphur binding domain
1	294	SUPERFAMILY	SSF54862	4Fe-4S ferredoxins
55	145	Pfam	PF13247	4Fe-4S dicluster domain
55	145	InterPro	IPR017896	4Fe-4S ferredoxin-type, iron-sulphur binding domain
78	107	ProSiteProfiles	PS51379	4Fe-4S ferredoxin-type iron-sulfur binding domain profile.
78	107	InterPro	IPR017896	4Fe-4S ferredoxin-type, iron-sulphur binding domain
87	98	ProSitePatterns	PS00198	4Fe-4S ferredoxin-type iron-sulfur binding region signature.
87	98	InterPro	IPR017900	4Fe-4S ferredoxin, iron-sulphur binding, conserved site
330	352	PRINTS	PR00419	Adrenodoxin reductase family signature
506	519	PRINTS	PR00419	Adrenodoxin reductase family signature
395	405	PRINTS	PR00419	Adrenodoxin reductase family signature
353	366	PRINTS	PR00419	Adrenodoxin reductase family signature
472	486	PRINTS	PR00419	Adrenodoxin reductase family signature
206	315	Pfam	PF14691	Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster
206	315	InterPro	IPR028261	Dihydroprymidine dehydrogenase domain II
117	653	PANTHER	PTHR42783	GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN
328	449	FunFam	G3DSA:3.50.50.60:FF:000077	Glutamate synthase small subunit
328	583	SUPERFAMILY	SSF51971	Nucleotide-binding domain
3	22	ProSiteProfiles	PS51379	4Fe-4S ferredoxin-type iron-sulfur binding domain profile.
3	22	InterPro	IPR017896	4Fe-4S ferredoxin-type, iron-sulphur binding domain
329	641	Pfam	PF07992	Pyridine nucleotide-disulphide oxidoreductase
329	641	InterPro	IPR023753	FAD/NAD(P)-binding domain
467	654	FunFam	G3DSA:3.50.50.60:FF:000068	Glutamate synthase small subunit
4	144	CDD	cd10554	HycB_like
5	174	Gene3D	G3DSA:3.30.70.20	-
429	582	Gene3D	G3DSA:3.50.50.60	-
429	582	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
181	326	Gene3D	G3DSA:1.10.1060.10	-
181	326	InterPro	IPR009051	Alpha-helical ferredoxin
62	120	Gene3D	G3DSA:3.30.70.20	-
327	370	Gene3D	G3DSA:3.50.50.60	-
327	370	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily

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 #1

0.937

Likely same site as P2Rank 1 4.1 Å 41 shared residues 95% of smaller site

Unusual size

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Surrounding area

Site 2 FPocket #37

0.612

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

0.931

Likely same site as FPocket 1 4.1 Å 41 shared residues 95% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.302

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Surrounding area

Site 3 P2Rank #3

0.265

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Surrounding area

Site 4 P2Rank #4

0.256

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Surrounding area

Site 5 P2Rank #5

0.248

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Surrounding area

Binding pockets · FPocket

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

Site 1 FPocket #1

0.957

Likely same site as P2Rank 1 3.9 Å 40 shared residues 83% of smaller site

Unusual size

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Surrounding area

Site 2 FPocket #42

0.285

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

0.944

Likely same site as FPocket 1 3.9 Å 40 shared residues 83% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.356

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Surrounding area

Site 3 P2Rank #3

0.302

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Surrounding area

Site 4 P2Rank #4

0.238

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Surrounding area

Site 5 P2Rank #5

0.228

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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_A0A0H3GWI5	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_03835	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.

58 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 8 records from similar proteins

Structural ligands 8 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

6MO PDB via homolog 95.9 Da · LogP -0.00 · TPSA 0.0 Open detail RCSB PDB

AKG PDB via homolog Detail RCSB PDB

CDL PDB via homolog Detail RCSB PDB

F3S PDB via homolog Detail RCSB PDB

FES 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
6MO RCSB PDB	1KQF	P0AAJ3	95.9 Da LogP -0.00 TPSA 0.0	✓ Ro5	✓ Clean	`[Mo+6]`
AKG RCSB PDB	2VDC	Q05756	146.1 Da LogP -0.50 TPSA 91.7	✓ Ro5	✓ Clean	`C(CC(=O)O)C(=O)C(=O)O`
CDL RCSB PDB	1KQF	P0AAJ3	1464.1 Da LogP 23.31 TPSA 242.6	3 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](COP(=O)([O-])OCC(…`
F3S RCSB PDB	2VDC	Q05756	295.8 Da LogP 2.59 TPSA 0.0	✓ Ro5	✓ Clean	`S1[Fe]2S[Fe]3[S]2[Fe]1S3`
FES RCSB PDB	5VJ7	I6V148	175.8 Da LogP 1.29 TPSA 0.0	✓ Ro5	✓ Clean	`S1[Fe]S[Fe]1`
HQO RCSB PDB	1KQG	P0AAJ3	259.3 Da LogP 3.69 TPSA 47.2	✓ Ro5	Alert	`CCCCCCCc1cc(c2ccccc2[n+]1[O-])O`
MGD RCSB PDB	1KQF	P0AAJ3	740.6 Da LogP -2.06 TPSA 346.6	3 viol.	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@@](=…`
OMT RCSB PDB	2VDC	Q05756	181.2 Da LogP -1.17 TPSA 97.5	✓ Ro5	✓ Clean	`CS(=O)(=O)CC[C@@H](C(=O)O)N`

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).

No ChEMBL hits found through similar proteins.

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
ZINC1529909 ZINC	1.000	259.3 Da LogP 3.69 TPSA 47.2	✓ Ro5	Alert	`CCCCCCCc1cc(O)c2ccccc2[n+]1[O-]`
ZINC102191119 ZINC	0.708	498.6 Da LogP 3.65 TPSA 148.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@@H](O)CO…`
ZINC58649551 ZINC	0.708	498.6 Da LogP 3.65 TPSA 148.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@H](O)CO)…`
ZINC36178999 ZINC	0.705	424.5 Da LogP 4.27 TPSA 119.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@@H](COP(=O)(O)O)OC(=O)CCCCCCC`
ZINC36179002 ZINC	0.705	424.5 Da LogP 4.27 TPSA 119.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](COP(=O)(O)O)OC(=O)CCCCCCC`
ZINC104869865 ZINC	0.684	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O…`
ZINC12504289 ZINC	0.684	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC34541308 ZINC	0.684	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC35000839 ZINC	0.684	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC45284491 ZINC	0.684	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC80639694 ZINC	0.684	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC8215481 ZINC	0.684	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC5820131 ZINC	0.682	368.4 Da LogP 2.71 TPSA 119.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](COP(=O)(O)O)OC(=O)CCCCC`
ZINC5820134 ZINC	0.682	368.4 Da LogP 2.71 TPSA 119.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](COP(=O)(O)O)OC(=O)CCCCC`
ZINC4521879 ZINC	0.650	386.5 Da LogP 4.73 TPSA 78.9	✓ Ro5	✓ Clean	`CCCCCC(=O)OCC(COC(=O)CCCCC)OC(=O)CCCCC`
ZINC137999083 ZINC	0.622	424.5 Da LogP 4.87 TPSA 113.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCCC(=O)OC[C@H](O)COP(=O)(O)O`
ZINC42851452 ZINC	0.622	424.5 Da LogP 4.87 TPSA 113.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCCC(=O)OC[C@@H](O)COP(=O)(O)O`
ZINC62624856 ZINC	0.622	382.4 Da LogP 3.70 TPSA 113.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@H](O)COP(=O)(O)O`
ZINC62624861 ZINC	0.622	382.4 Da LogP 3.70 TPSA 113.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@@H](O)COP(=O)(O)O`
ZINC8218993 ZINC	0.622	410.5 Da LogP 4.48 TPSA 113.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](O)COP(=O)(O)O`
ZINC8219000 ZINC	0.622	410.5 Da LogP 4.48 TPSA 113.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@@H](O)COP(=O)(O)O`
ZINC102190506 ZINC	0.620	467.5 Da LogP 4.25 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OCCN)OC(=O)CC…`
ZINC102190512 ZINC	0.620	467.5 Da LogP 4.25 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)C…`
ZINC12501413 ZINC	0.610	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)…`
ZINC12958448 ZINC	0.610	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](COP(=O)(O)O)[C@H](O)[…`
ZINC1532555 ZINC	0.610	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[…`
ZINC16546189 ZINC	0.610	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](COP(=O)(O)O)[C@H](O)[…`
ZINC2159505 ZINC	0.610	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)…`
ZINC3073318 ZINC	0.610	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)…`
ZINC3869963 ZINC	0.610	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)…`
ZINC3869965 ZINC	0.610	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@@H](COP(=O)(O)O)[C@@H](O…`
ZINC9334496 ZINC	0.610	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[…`
ZINC19429847 ZINC	0.607	208.3 Da LogP -1.16 TPSA 80.5	✓ Ro5	✓ Clean	`CN(C)C(=O)[C@@H](N)CCS(C)(=O)=O`
ZINC19429848 ZINC	0.607	208.3 Da LogP -1.16 TPSA 80.5	✓ Ro5	✓ Clean	`CN(C)C(=O)[C@H](N)CCS(C)(=O)=O`
ZINC26513844 ZINC	0.607	209.3 Da LogP -0.69 TPSA 86.5	✓ Ro5	✓ Clean	`CCOC(=O)[C@@H](N)CCS(C)(=O)=O`
ZINC26513846 ZINC	0.607	209.3 Da LogP -0.69 TPSA 86.5	✓ Ro5	✓ Clean	`CCOC(=O)[C@H](N)CCS(C)(=O)=O`
ZINC13552119 ZINC	0.600	270.2 Da LogP 0.58 TPSA 113.3	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](O)COP(=O)(O)O`
ZINC27416437 ZINC	0.600	411.4 Da LogP 2.69 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCCN)OC(=O)CCCCC`
ZINC33902364 ZINC	0.600	411.4 Da LogP 2.69 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)CCC…`
ZINC36079847 ZINC	0.591	344.5 Da LogP 4.15 TPSA 72.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@@H](CO)OC(=O)CCCCCCC`
ZINC8214428 ZINC	0.591	344.5 Da LogP 4.15 TPSA 72.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO)OC(=O)CCCCCCC`
ZINC13543394 ZINC	0.588	455.4 Da LogP 2.15 TPSA 171.7	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@H](N)C(=O)…`
ZINC4521911 ZINC	0.585	344.4 Da LogP 3.56 TPSA 78.9	✓ Ro5	✓ Clean	`CCCCC(=O)OCC(COC(=O)CCCC)OC(=O)CCCC`
ZINC85603366 ZINC	0.585	344.5 Da LogP 4.15 TPSA 72.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OCC(O)COC(=O)CCCCCCC`
ZINC13544781 ZINC	0.585	482.6 Da LogP 4.22 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)OC[C@@H](CO[P@](=O)(O)OCC[N+](C)(C)C…`
ZINC13544783 ZINC	0.585	482.6 Da LogP 4.22 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCC[N+](C)(C)C)…`
ZINC102191158 ZINC	0.571	456.5 Da LogP 3.08 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@@](=O)(O)OC[C@…`
ZINC14880758 ZINC	0.571	484.6 Da LogP 3.86 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@](=O)(O)OC[…`
ZINC62592203 ZINC	0.571	456.5 Da LogP 3.08 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@@](=O)(O)OC[C…`
ZINC96094841 ZINC	0.571	456.5 Da LogP 3.08 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@@](=O)(O)OC[C…`

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.