KpKP13 Protein target profile

DNA polymerase III subunit beta

Accession: KP13_00049

Gene: dnaN AHE41973.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GV83

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Length 366

Pocket druggability (P2Rank · AlphaFold DB model) 0.04

Direct ligand evidence 0 74 total records

Functional annotation 0 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

Risks to review

Microbiome similarity 164 of 4744 screened genomes (3.5%) have a significant similarity hit. Weak predicted binding pocket FPocket selected-pocket score 0.23. Weak second pocket-predictor signal P2Rank predicted binding-site probability 0.04.

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: No hit
Gut microbiome similarity: 3.5% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 96.995 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 96.59 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

P2Rank's binding-site probability is the primary druggability signal shown across the app; FPocket's druggability score is shown alongside it for comparison. Both estimate small-molecule pocket quality after applying the curated structure priority — neither is experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

Druggability (P2Rank) 0.04

Structure A0A0H3GV83

Pocket Pocket 1

Druggability (FPocket) 0.232

Structure A0A0H3GV83

Pocket Pocket 15

ColabFold model

P2Rank 0.029 · Pocket 1

FPocket 0.617 · Pocket 7

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 164 / 4744 genomes with a hit

Prevalence 3.5%

Cross-references

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

Sequence

UniProt A0A0H3GV83

Chemistry

ChEMBL CHEMBL3577268 ChEMBL CHEMBL3577269 ChEMBL CHEMBL3577272 ChEMBL CHEMBL3577289 ChEMBL CHEMBL3577290

Sequence

Primary amino-acid sequence viewer.

MKFTVEREHLLKPLQQVSGPLGGRPTLPILGNLLLQVADGALSLTGTDLEMEMVARVALVQPHEAGATTVPARKFFDICRGLPEGAEIAVQLEGDRMLVRSGRSRFSLSTLPAADFPNLDDWQSEVEFTLPQATMKRLIEATQFSMAHQDVRYYLNGMLFETEGSELRTVATDGHRLAVCSMPLEASLPNHSVIVPRKGVIELMRMLDGGDTPLRVQIGSNNIRAHVGDFIFTSKLVDGRFPDYRRVLPKNPDKHLEAGCDILKQAFARAAILSNEKFRGVRLYVSENQLKITANNPEQEEAEEILDVTYAGTEMEIGFNVSYVLDVLNALKCENVRILLTDSVSSVQIEDAASQSAAYVVMPMRL

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

8 GO

Subcellular localization

Localization: Cytoplasmic

Gene Ontology (GO)

GO:0009360 The DNA polymerase III holoenzyme is a complex that contains 10 different types of subunits. These subunits are organized into 3 functionally essential sub-assemblies: the pol III core, the beta sliding clamp processivity factor and the clamp-loading complex. The pol III core carries out the polymerase and the 3'-5' exonuclease proofreading activities. The polymerase is tethered to the template via the sliding clamp processivity factor. The clamp-loading complex assembles the beta processivity factor onto the primer template and plays a central role in the organization and communication at the replication fork.
GO:0006260 The cellular metabolic process in which a cell duplicates one or more molecules of DNA. DNA replication begins when specific sequences, known as origins of replication, are recognized and bound by the origin recognition complex, and ends when the original DNA molecule has been completely duplicated and the copies topologically separated. The unit of replication usually corresponds to the genome of the cell, an organelle, or a virus. The template for replication can either be an existing DNA molecule or RNA.
GO:0003887 Catalysis of the reaction: deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1); DNA-template-directed extension of the 3'-end of a DNA strand by one nucleotide at a time.
GO:0008408 Catalysis of the hydrolysis of ester linkages within nucleic acids by removing nucleotide residues from the 3' end.
GO:0003677 Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0042802 Binding to an identical protein or proteins.
GO:0006271 The process in which an existing DNA strand is extended by activities including the addition of nucleotides to the 3' end of the strand, complementary to an existing template, as part of DNA replication.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

26 records

Show feature table

Start	End	DB	Term	Name
248	366	FunFam	G3DSA:3.10.150.10:FF:000003	Beta sliding clamp
1	365	CDD	cd00140	beta_clamp
1	365	InterPro	IPR001001	DNA polymerase III, beta sliding clamp
1	366	PANTHER	PTHR30478	DNA POLYMERASE III SUBUNIT BETA
1	366	InterPro	IPR001001	DNA polymerase III, beta sliding clamp
17	362	SMART	SM00480	pol35
17	362	InterPro	IPR001001	DNA polymerase III, beta sliding clamp
1	366	PIRSF	PIRSF000804	DNA_pol_III_b
1	121	SUPERFAMILY	SSF55979	DNA clamp
1	121	InterPro	IPR046938	DNA clamp superfamily
1	123	FunFam	G3DSA:3.10.150.10:FF:000001	Beta sliding clamp
124	247	Gene3D	G3DSA:3.10.150.10	DNA Polymerase III, subunit A, domain 2
124	247	FunFam	G3DSA:3.10.150.10:FF:000002	Beta sliding clamp
1	366	NCBIfam	TIGR00663	DNA polymerase III subunit beta
129	243	Pfam	PF02767	DNA polymerase III beta subunit, central domain
129	243	InterPro	IPR022637	DNA polymerase III, beta sliding clamp, central
1	120	Pfam	PF00712	DNA polymerase III beta subunit, N-terminal domain
1	120	InterPro	IPR022634	DNA polymerase III, beta sliding clamp, N-terminal
245	366	SUPERFAMILY	SSF55979	DNA clamp
245	366	InterPro	IPR046938	DNA clamp superfamily
248	366	Gene3D	G3DSA:3.10.150.10	DNA Polymerase III, subunit A, domain 2
1	123	Gene3D	G3DSA:3.10.150.10	DNA Polymerase III, subunit A, domain 2
125	244	SUPERFAMILY	SSF55979	DNA clamp
125	244	InterPro	IPR046938	DNA clamp superfamily
245	365	Pfam	PF02768	DNA polymerase III beta subunit, C-terminal domain
245	365	InterPro	IPR022635	DNA polymerase III, beta sliding clamp, C-terminal

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 · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.04

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Surrounding area

Pocket 2 P2Rank #2

0.008

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Surrounding area

Pocket 3 P2Rank #3

0.0

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Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #15

0.232

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Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #7

0.617

Likely same site as P2Rank 1 1.3 Å 9 shared residues 100% of smaller site

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Surrounding area

Pocket 2 FPocket #9

0.376 Unusual size

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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_A0A0H3GV83	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_00049	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.

74 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 24 records from similar proteins

Structural ligands 19 0 loaded crystals

Measured bioactivity 5 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

0LA PDB via homolog 273.7 Da · LogP 4.16 · TPSA 53.1 Open detail RCSB PDB

1FL PDB via homolog Detail RCSB PDB

27O PDB via homolog Detail RCSB PDB

27R PDB via homolog Detail RCSB PDB

2HO 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
0LA RCSB PDB	4MJR	P0A988	273.7 Da LogP 4.16 TPSA 53.1	✓ Ro5	✓ Clean	`C[C@@H](c1ccc2c3cc(ccc3[nH]c2c1)Cl)C(=O)O`
1FL RCSB PDB	5G48	O25242	250.2 Da LogP 3.04 TPSA 57.5	✓ Ro5	✓ Clean	`c1cc(c(cc1c2ccc(cc2F)F)C(=O)O)O`
27O RCSB PDB	4MJP	P0A988	282.4 Da LogP 5.08 TPSA 37.3	1 viol.	✓ Clean	`C[C@H](c1ccc(c2c1cccc2)C3CCCCC3)C(=O)O`
27R RCSB PDB	4MJQ	P0A988	334.2 Da LogP 2.89 TPSA 80.4	✓ Ro5	Alert	`c1cc(c(c(c1)C(=O)c2ccc(cc2)Br)N)CC(=O)O`
2HO RCSB PDB	4N94	P0A988	157.1 Da LogP 1.06 TPSA 43.1	✓ Ro5	✓ Clean	`c1cc(c(cc1C(=O)N)F)F`
2HQ RCSB PDB	4N95	P0A988	181.6 Da LogP 1.47 TPSA 46.2	✓ Ro5	✓ Clean	`c1cc2c(cc1Cl)C(=O)C(=O)N2`
2HU RCSB PDB	4N97	P0A988	162.1 Da LogP 2.08 TPSA 58.9	✓ Ro5	✓ Clean	`c1cc2c(cc[nH]2)cc1[N+](=O)[O-]`
2J1 RCSB PDB	4N99	P0A988	249.7 Da LogP 3.40 TPSA 53.1	✓ Ro5	Alert	`c1c2c(cc(c1Cl)C(=O)O)[nH]c3c2CCCC3`
2J2 RCSB PDB	4N9A	P0A988	249.7 Da LogP 3.33 TPSA 53.1	✓ Ro5	✓ Clean	`c1cc2c(cc1Cl)c3c([nH]2)[C@@H](CCC3)C(=O)O`
322 RCSB PDB	3D1G	P0A988	499.2 Da LogP 3.17 TPSA 87.1	✓ Ro5	Alert	`CCOc1cc(c(c(c1O)Br)Br)C[C@@H]2C(=O)N(C(=S)S2)CC…`
323 RCSB PDB	3D1F	P0A988	414.5 Da LogP 2.48 TPSA 76.6	✓ Ro5	✓ Clean	`CN(C)c1ccc2c(c1)OC3=CC(=[N+](C)C)C=CC3=C2c4ccc(…`
4FC RCSB PDB	4N98	P0A988	216.2 Da LogP 3.19 TPSA 37.3	✓ Ro5	✓ Clean	`c1cc(ccc1c2ccc(cc2)F)C(=O)O`
5CY RCSB PDB	3BEP	P0A988	471.7 Da LogP 5.62 TPSA 46.7	1 viol.	✓ Clean	`CC1(c2ccccc2[N+](=C1/C=C/C=C/C=C/3\C(c4ccccc4N3…`
6NI RCSB PDB	4N96	P0A988	163.1 Da LogP 1.47 TPSA 71.8	✓ Ro5	✓ Clean	`c1cc2cn[nH]c2cc1[N+](=O)[O-]`
743 RCSB PDB	3QSB	P0A988	434.5 Da LogP 5.49 TPSA 79.5	1 viol.	✓ Clean	`CCCC(=NOCc1ccc(cc1)c2ccc(cc2)F)C3C(=O)CC(C(C3=O…`
BU3 RCSB PDB	5AGV	P9WNU1	90.1 Da LogP -0.25 TPSA 40.5	✓ Ro5	✓ Clean	`C[C@H]([C@@H](C)O)O`
MLU RCSB PDB	5AGU	P9WNU1	145.2 Da LogP 0.71 TPSA 49.3	✓ Ro5	✓ Clean	`CC(C)C[C@H](C(=O)O)NC`
P4C RCSB PDB	4K3S	P0A988	324.4 Da LogP -0.72 TPSA 92.7	✓ Ro5	✓ Clean	`C(COCCOCCOCCOCCOCCOCC=O)O`
SFK RCSB PDB	4K3K	P0A988	263.3 Da LogP 2.23 TPSA 66.4	✓ Ro5	✓ Clean	`CC(C)CCC(=O)N[C@@H](Cc1ccccc1)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
CHEMBL3577268 ChEMBL	P0A988	—	249.7 Da LogP 3.01 TPSA 53.1	✓ Ro5	Alert	`O=C(O)[C@@H]1CCc2c([nH]c3ccc(Cl)cc23)C1`
CHEMBL3577269 ChEMBL	P0A988	—	249.7 Da LogP 3.01 TPSA 53.1	✓ Ro5	Alert	`O=C(O)[C@H]1CCc2c([nH]c3ccc(Cl)cc23)C1`
CHEMBL3577272 ChEMBL	P0A988	—	294.1 Da LogP 3.12 TPSA 53.1	✓ Ro5	Alert	`O=C(O)[C@@H]1CCc2c([nH]c3ccc(Br)cc23)C1`
CHEMBL3577289 ChEMBL	P0A988	—	499.4 Da LogP 3.41 TPSA 108.6	✓ Ro5	Alert	`O=C(Cn1c2c(c3cc(Br)ccc31)CC[C@@H](C(=O)O)C2)N[C…`
CHEMBL3577290 ChEMBL	P0A988	—	499.4 Da LogP 3.41 TPSA 108.6	✓ Ro5	Alert	`O=C(Cn1c2c(c3cc(Br)ccc31)CC[C@@H](C(=O)O)C2)N[C…`

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
ZINC117391805 ZINC	1.000	294.1 Da LogP 3.12 TPSA 53.1	✓ Ro5	Alert	`O=C(O)[C@@H]1CCc2c([nH]c3ccc(Br)cc23)C1`
ZINC117391807 ZINC	1.000	294.1 Da LogP 3.12 TPSA 53.1	✓ Ro5	Alert	`O=C(O)[C@H]1CCc2c([nH]c3ccc(Br)cc23)C1`
ZINC1869694 ZINC	1.000	273.7 Da LogP 4.16 TPSA 53.1	✓ Ro5	✓ Clean	`C[C@@H](C(=O)O)c1ccc2c(c1)[nH]c1ccc(Cl)cc12`
ZINC20235 ZINC	1.000	273.7 Da LogP 4.16 TPSA 53.1	✓ Ro5	✓ Clean	`C[C@H](C(=O)O)c1ccc2c(c1)[nH]c1ccc(Cl)cc12`
ZINC20249400 ZINC	1.000	263.3 Da LogP 2.23 TPSA 66.4	✓ Ro5	✓ Clean	`CC(C)CCC(=O)N[C@@H](Cc1ccccc1)C(=O)O`
ZINC20249402 ZINC	1.000	263.3 Da LogP 2.23 TPSA 66.4	✓ Ro5	✓ Clean	`CC(C)CCC(=O)N[C@H](Cc1ccccc1)C(=O)O`
ZINC2382451 ZINC	1.000	216.2 Da LogP 3.19 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)c1ccc(-c2ccc(F)cc2)cc1`
ZINC2570817 ZINC	1.000	334.2 Da LogP 2.89 TPSA 80.4	✓ Ro5	Alert	`Nc1c(CC(=O)O)cccc1C(=O)c1ccc(Br)cc1`
ZINC340258 ZINC	1.000	249.7 Da LogP 3.33 TPSA 53.1	✓ Ro5	✓ Clean	`O=C(O)[C@H]1CCCc2c1[nH]c1ccc(Cl)cc21`
ZINC4018831 ZINC	1.000	249.7 Da LogP 3.33 TPSA 53.1	✓ Ro5	✓ Clean	`O=C(O)[C@@H]1CCCc2c1[nH]c1ccc(Cl)cc21`
ZINC807911 ZINC	1.000	249.7 Da LogP 3.40 TPSA 53.1	✓ Ro5	Alert	`O=C(O)c1cc2[nH]c3c(c2cc1Cl)CCCC3`
ZINC575319668 ZINC	0.923	263.7 Da LogP 3.72 TPSA 53.1	✓ Ro5	✓ Clean	`O=C(O)[C@H]1CCCCc2c1[nH]c1ccc(Cl)cc21`
ZINC575319669 ZINC	0.923	263.7 Da LogP 3.72 TPSA 53.1	✓ Ro5	✓ Clean	`O=C(O)[C@@H]1CCCCc2c1[nH]c1ccc(Cl)cc21`
ZINC49837746 ZINC	0.810	249.7 Da LogP 3.01 TPSA 53.1	✓ Ro5	Alert	`O=C(O)[C@H]1CCc2[nH]c3ccc(Cl)cc3c2C1`
ZINC49837747 ZINC	0.810	249.7 Da LogP 3.01 TPSA 53.1	✓ Ro5	Alert	`O=C(O)[C@@H]1CCc2[nH]c3ccc(Cl)cc3c2C1`
ZINC93985 ZINC	0.786	248.7 Da LogP 2.73 TPSA 58.9	✓ Ro5	✓ Clean	`NC(=O)[C@H]1CCCc2c1[nH]c1ccc(Cl)cc21`
ZINC93989 ZINC	0.786	248.7 Da LogP 2.73 TPSA 58.9	✓ Ro5	✓ Clean	`NC(=O)[C@@H]1CCCc2c1[nH]c1ccc(Cl)cc21`
ZINC909 ZINC	0.765	255.3 Da LogP 2.13 TPSA 80.4	✓ Ro5	Alert	`Nc1c(CC(=O)O)cccc1C(=O)c1ccccc1`
ZINC11891070 ZINC	0.750	249.3 Da LogP 1.84 TPSA 66.4	✓ Ro5	✓ Clean	`CC(C)CC(=O)N[C@@H](Cc1ccccc1)C(=O)O`
ZINC11891072 ZINC	0.750	249.3 Da LogP 1.84 TPSA 66.4	✓ Ro5	✓ Clean	`CC(C)CC(=O)N[C@H](Cc1ccccc1)C(=O)O`
ZINC134079 ZINC	0.750	242.2 Da LogP 2.75 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)c1ccc(-c2ccc(C(=O)O)cc2)cc1`
ZINC3147211 ZINC	0.750	318.3 Da LogP 4.42 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)c1ccc(-c2ccc(-c3ccc(C(=O)O)cc3)cc2)cc1`
ZINC15261553 ZINC	0.737	294.3 Da LogP -0.01 TPSA 129.7	✓ Ro5	✓ Clean	`N[C@H](CCC(=O)N[C@@H](Cc1ccccc1)C(=O)O)C(=O)O`
ZINC15261555 ZINC	0.737	294.3 Da LogP -0.01 TPSA 129.7	✓ Ro5	✓ Clean	`N[C@@H](CCC(=O)N[C@H](Cc1ccccc1)C(=O)O)C(=O)O`
ZINC15261557 ZINC	0.737	294.3 Da LogP -0.01 TPSA 129.7	✓ Ro5	✓ Clean	`N[C@H](CCC(=O)N[C@H](Cc1ccccc1)C(=O)O)C(=O)O`
ZINC2242693 ZINC	0.737	294.3 Da LogP -0.01 TPSA 129.7	✓ Ro5	✓ Clean	`N[C@@H](CCC(=O)N[C@@H](Cc1ccccc1)C(=O)O)C(=O)O`
ZINC16946243 ZINC	0.733	257.7 Da LogP 3.14 TPSA 46.2	✓ Ro5	✓ Clean	`O=C1Nc2ccc(-c3ccc(Cl)cc3)cc2C1=O`
ZINC53542 ZINC	0.733	263.7 Da LogP 3.41 TPSA 42.1	✓ Ro5	✓ Clean	`COC(=O)[C@H]1CCCc2c1[nH]c1ccc(Cl)cc21`
ZINC53543 ZINC	0.733	263.7 Da LogP 3.41 TPSA 42.1	✓ Ro5	✓ Clean	`COC(=O)[C@@H]1CCCc2c1[nH]c1ccc(Cl)cc21`
ZINC5161668 ZINC	0.730	289.7 Da LogP 2.78 TPSA 80.4	✓ Ro5	Alert	`Nc1c(CC(=O)O)cccc1C(=O)c1ccc(Cl)cc1`
ZINC499303 ZINC	0.727	262.7 Da LogP 3.12 TPSA 58.9	✓ Ro5	✓ Clean	`NC(=O)[C@H]1CCCCc2c1[nH]c1ccc(Cl)cc21`
ZINC499304 ZINC	0.727	262.7 Da LogP 3.12 TPSA 58.9	✓ Ro5	✓ Clean	`NC(=O)[C@@H]1CCCCc2c1[nH]c1ccc(Cl)cc21`
ZINC1598043 ZINC	0.722	236.3 Da LogP 0.15 TPSA 92.4	✓ Ro5	✓ Clean	`NCCC(=O)N[C@H](Cc1ccccc1)C(=O)O`
ZINC1845204 ZINC	0.722	297.4 Da LogP 2.43 TPSA 66.4	✓ Ro5	✓ Clean	`O=C(CCc1ccccc1)N[C@H](Cc1ccccc1)C(=O)O`
ZINC1845206 ZINC	0.722	297.4 Da LogP 2.43 TPSA 66.4	✓ Ro5	✓ Clean	`O=C(CCc1ccccc1)N[C@@H](Cc1ccccc1)C(=O)O`
ZINC2545129 ZINC	0.722	236.3 Da LogP 0.15 TPSA 92.4	✓ Ro5	✓ Clean	`NCCC(=O)N[C@@H](Cc1ccccc1)C(=O)O`
ZINC3175547 ZINC	0.722	265.3 Da LogP 0.66 TPSA 103.7	✓ Ro5	✓ Clean	`O=C(O)CCC(=O)N[C@@H](Cc1ccccc1)C(=O)O`
ZINC3175549 ZINC	0.722	265.3 Da LogP 0.66 TPSA 103.7	✓ Ro5	✓ Clean	`O=C(O)CCC(=O)N[C@H](Cc1ccccc1)C(=O)O`
ZINC128690 ZINC	0.721	294.1 Da LogP 3.43 TPSA 53.1	✓ Ro5	✓ Clean	`O=C(O)[C@H]1CCCc2c1[nH]c1ccc(Br)cc21`
ZINC128692 ZINC	0.721	294.1 Da LogP 3.43 TPSA 53.1	✓ Ro5	✓ Clean	`O=C(O)[C@@H]1CCCc2c1[nH]c1ccc(Br)cc21`
ZINC3683849 ZINC	0.721	229.3 Da LogP 2.98 TPSA 53.1	✓ Ro5	✓ Clean	`Cc1ccc2[nH]c3c(c2c1)CCC[C@@H]3C(=O)O`
ZINC3683850 ZINC	0.721	229.3 Da LogP 2.98 TPSA 53.1	✓ Ro5	✓ Clean	`Cc1ccc2[nH]c3c(c2c1)CCC[C@H]3C(=O)O`
ZINC2513032 ZINC	0.720	234.2 Da LogP 3.33 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)c1ccc(-c2cc(F)cc(F)c2)cc1`
ZINC1677646 ZINC	0.714	221.3 Da LogP 1.21 TPSA 66.4	✓ Ro5	✓ Clean	`CCC(=O)N[C@@H](Cc1ccccc1)C(=O)O`
ZINC6655209 ZINC	0.714	221.3 Da LogP 1.21 TPSA 66.4	✓ Ro5	✓ Clean	`CCC(=O)N[C@H](Cc1ccccc1)C(=O)O`
ZINC22054172 ZINC	0.711	301.8 Da LogP 4.64 TPSA 42.1	✓ Ro5	✓ Clean	`CCOC(=O)[C@@H](C)c1ccc2c(c1)[nH]c1ccc(Cl)cc12`
ZINC22054176 ZINC	0.711	301.8 Da LogP 4.64 TPSA 42.1	✓ Ro5	✓ Clean	`CCOC(=O)[C@H](C)c1ccc2c(c1)[nH]c1ccc(Cl)cc12`
ZINC11891064 ZINC	0.711	249.3 Da LogP 1.99 TPSA 66.4	✓ Ro5	✓ Clean	`CCCCC(=O)N[C@@H](Cc1ccccc1)C(=O)O`
ZINC11891067 ZINC	0.711	249.3 Da LogP 1.99 TPSA 66.4	✓ Ro5	✓ Clean	`CCCCC(=O)N[C@H](Cc1ccccc1)C(=O)O`
ZINC757568599 ZINC	0.704	233.2 Da LogP 2.73 TPSA 43.1	✓ Ro5	✓ Clean	`NC(=O)c1ccc(-c2ccc(F)c(F)c2)cc1`

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.