KpKP13 Protein target profile

Oligopeptidase A

Accession: KP13_00308

Gene: prlC AHE42217.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GZT5

Export view

Length 680

Pocket druggability (P2Rank · AlphaFold DB model) 0.997

Direct ligand evidence 0 57 total records

Functional annotation 1 EC 7 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: P2Rank + FPocket Both predictors report a high-scoring binding site (P2Rank 1.00, FPocket 0.84). Use the 3D pocket comparison to verify whether they identify the same site. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Strong predicted binding pocket FPocket selected-pocket score 0.84. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 1.00. 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 (%): 41.436 Lower values reduce human off-target concern.
Human E-value: 2.25e-36
Gut microbiome similarity: 4.0% 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.

Structure confidence

ColabFold pLDDT: 96.65 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) 0.997

Structure A0A0H3GZT5

Pocket Pocket 1

Druggability (FPocket) 0.84

Structure A0A0H3GZT5

Pocket Pocket 2

ColabFold model

P2Rank 0.997 · Pocket 1

FPocket 0.83 · Pocket 23

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 188 / 4744 genomes with a hit

Prevalence 4.0%

Sequence

Primary amino-acid sequence viewer.

MTNPLLTPFSLPPFSAIKPEHVVPAVTKALEDCRAAVESAVAHGAPYSWENLCQPLAEVDDVLGRIFSPVSHLNSVKNSPELREAYEQTLPLLSEYSTWVGQHEGLYKAYRDLRDGDNYATLNTAQKKAVDNALRDFELSGIGLPPEAQKRYGEIAARLSELGNQYSNNVLDATMGWNKLVTDVADLAGMPESALAAAQAQAQAKEQEGYLLTLDIPSYLPVMTYCDNQALREEMYRAYSTRASDQGPNAGKWDNSPVMAEILALRHELAQLLGFDSYAYKSLATKMAKDPQQVLDFLTDLAKRARPQGEKELAQLRAFAKAEFGVDELQPWDIAYYSEKQKQHLYSISDEQLRPYFPENKAVSGLFEVVKRIYGITAKERTDVDVWHPEVRFFELYDEHNELRGSFYLDLYAREHKRGGAWMDDCVGQMRKLDGSLQKPVAYLTCNFNRPVNGKPALFTHDEVITLFHEFGHGLHHMLTRIDTAGVSGISGVPWDAVELPSQFMENWCWEPEALAFISGHYETGEPLPQELLEKMLAAKNYQAAMFILRQLEFGLFDFRLHAEYKPEQGAKILETLAEIKKQVAVVPGPTWGRFPHAFSHIFAGGYAAGYYSYLWADVLAADAFSRFEEEGIFNRETGQSFLDNILSRGGSEEPMELFKRFRGREPQLDAMLEHYGIKG

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

3.4.24.70

Gene Ontology (GO)

GO:0004222 Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.
GO:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
GO:0008233 Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid.
GO:0008237 Catalysis of the hydrolysis of peptide bonds by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0046872 Binding to a metal ion.
GO:0006518 The chemical reactions and pathways involving peptides, compounds of two or more amino acids where the alpha carboxyl group of one is bound to the alpha amino group of another.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

14 records

Show feature table

Start	End	DB	Term	Name
358	508	Gene3D	G3DSA:3.40.390.10	Collagenase (Catalytic Domain)
358	508	InterPro	IPR024079	Metallopeptidase, catalytic domain superfamily
3	679	PANTHER	PTHR11804	PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED
3	679	InterPro	IPR045090	Peptidase M3A/M3B
358	508	FunFam	G3DSA:3.40.390.10:FF:000009	Oligopeptidase A
20	678	CDD	cd06456	M3A_DCP
20	678	InterPro	IPR034005	Peptidyl-dipeptidase DCP
1	677	SUPERFAMILY	SSF55486	Metalloproteases ("zincins"), catalytic domain
150	673	Gene3D	G3DSA:1.10.1370.10	Neurolysin, domain 3
150	673	InterPro	IPR024077	Neurolysin/Thimet oligopeptidase, domain 2
222	677	Pfam	PF01432	Peptidase family M3
222	677	InterPro	IPR001567	Peptidase M3A/M3B catalytic domain
35	147	Pfam	PF19310	Neurolysin/Thimet oligopeptidase, N-terminal domain
35	147	InterPro	IPR045666	Oligopeptidase A, 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.

Download VMD script Full viewer

Loading 3D structure...

Drag to rotate — click the view, then scroll to zoom.

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

0.997

Show in viewer

Surrounding area

Pocket 2 P2Rank #2

0.869

Show in viewer

Surrounding area

Pocket 3 P2Rank #3

0.46

Show in viewer

Surrounding area

Pocket 4 P2Rank #4

0.387

Show in viewer

Surrounding area

Pocket 5 P2Rank #5

0.293

Likely same site as FPocket 37 0.9 Å 8 shared residues 100% of smaller site

Show in viewer

Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #2

0.84 Unusual size

Show in viewer

Surrounding area

Pocket 2 FPocket #37

0.398

Likely same site as P2Rank 5 0.9 Å 8 shared residues 100% of smaller site

Show in viewer

Surrounding area

Pocket 3 FPocket #44

0.22 Unusual size

Show in viewer

Surrounding area

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.997

Show in viewer

Surrounding area

Pocket 2 P2Rank #2

0.826

Show in viewer

Surrounding area

Pocket 3 P2Rank #3

0.512

Show in viewer

Surrounding area

Pocket 4 P2Rank #4

0.356

Show in viewer

Surrounding area

Pocket 5 P2Rank #5

0.336

Likely same site as FPocket 36 1.1 Å 8 shared residues 100% of smaller site

Show in viewer

Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #23

0.83 Unusual size

Show in viewer

Surrounding area

Pocket 2 FPocket #1

0.703 Unusual size

Show in viewer

Surrounding area

Pocket 3 FPocket #36

0.268

Likely same site as P2Rank 5 1.1 Å 8 shared residues 100% of smaller site

Show in viewer

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_A0A0H3GZT5	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_00308	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.

57 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 7 records from similar proteins

Structural ligands 2 0 loaded crystals

Measured bioactivity 5 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

0W2 PDB via homolog 525.1 Da · LogP 5.69 · TPSA 64.7 Open detail RCSB PDB

K26 PDB via homolog Detail RCSB PDB

DWT ChEMBL via homolog · pchembl 6.97 (~107.2 nM) Detail ChEMBL

CHEMBL5070123 ChEMBL via homolog · pchembl 6.00 (~1.0 µM) Detail ChEMBL

CHEMBL5079973 ChEMBL via homolog Detail ChEMBL

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
0W2 RCSB PDB	4FXY	P42676	525.1 Da LogP 5.69 TPSA 64.7	2 viol.	✓ Clean	`C[C@@H](C(=O)N1CC[C@@H](N1c2ccccc2F)c3ccccc3Cl)…`
K26 RCSB PDB	5L44	A0A1L1QK30	535.5 Da LogP 1.54 TPSA 185.3	2 viol.	✓ Clean	`CC[C@H](C)[C@@H](C(=O)N[C@@H](Cc1ccc(cc1)O)C(=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
DWT ChEMBL	Q9BYT8	6.97 ~107.2 nM	503.5 Da LogP 5.75 TPSA 97.6	2 viol.	✓ Clean	`Cc1ccc(cc1Nc2c3cn(nc3nc(n2)c4cccnc4)C)C(=O)Nc5c…`
CHEMBL5070123 ChEMBL	P42676	6.00 ~1.0 µM	297.4 Da LogP 1.12 TPSA 99.6	✓ Ro5	✓ Clean	`N[C@H](Cc1c[nH]cn1)C(=O)NCCc1cc2ccccc2[nH]1`
CHEMBL5079973 ChEMBL	P52888	—	297.4 Da LogP 1.12 TPSA 99.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]cn1)C(=O)NCCc1cc2ccccc2[nH]1`
CHEMBL5092803 ChEMBL	P42676	—	294.4 Da LogP 1.75 TPSA 83.8	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]cn1)C(=O)NCc1cccc2ccccc12`
CHEMBL5284556 ChEMBL	P42676	—	295.3 Da LogP 1.14 TPSA 96.7	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]cn1)C(=O)NCc1cccc2cccnc12`

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
ZINC4899521 ZINC	0.778	203.2 Da LogP 0.52 TPSA 84.9	✓ Ro5	✓ Clean	`NC(=O)[C@H](N)Cc1c[nH]c2ccccc12`
ZINC57505 ZINC	0.778	203.2 Da LogP 0.52 TPSA 84.9	✓ Ro5	✓ Clean	`NC(=O)[C@@H](N)Cc1c[nH]c2ccccc12`
ZINC2566035 ZINC	0.757	218.3 Da LogP 1.51 TPSA 79.1	✓ Ro5	✓ Clean	`N[C@@H](CCc1c[nH]c2ccccc12)C(=O)O`
ZINC6864822 ZINC	0.757	218.3 Da LogP 1.51 TPSA 79.1	✓ Ro5	✓ Clean	`N[C@H](CCc1c[nH]c2ccccc12)C(=O)O`
ZINC1690614 ZINC	0.743	233.2 Da LogP 1.50 TPSA 90.4	✓ Ro5	✓ Clean	`O=C(O)C(Cc1c[nH]c2ccccc12)C(=O)O`
ZINC14982898 ZINC	0.711	220.2 Da LogP 0.83 TPSA 99.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]c2c(O)cccc12)C(=O)O`
ZINC14982901 ZINC	0.711	220.2 Da LogP 0.83 TPSA 99.3	✓ Ro5	✓ Clean	`N[C@H](Cc1c[nH]c2c(O)cccc12)C(=O)O`
ZINC35051054 ZINC	0.707	294.4 Da LogP 2.78 TPSA 68.1	✓ Ro5	✓ Clean	`N[C@H](Cc1c[nH]c2ccccc12)C(=O)OCc1ccccc1`
ZINC35051056 ZINC	0.707	294.4 Da LogP 2.78 TPSA 68.1	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]c2ccccc12)C(=O)OCc1ccccc1`
ZINC39098 ZINC	0.703	205.2 Da LogP 1.16 TPSA 73.3	✓ Ro5	✓ Clean	`O=C(O)[C@@H](O)Cc1c[nH]c2ccccc12`
ZINC39099 ZINC	0.703	205.2 Da LogP 1.16 TPSA 73.3	✓ Ro5	✓ Clean	`O=C(O)[C@H](O)Cc1c[nH]c2ccccc12`
ZINC83138991 ZINC	0.703	268.1 Da LogP 2.56 TPSA 53.1	✓ Ro5	✓ Clean	`O=C(O)[C@@H](Br)Cc1c[nH]c2ccccc12`
ZINC52968847 ZINC	0.700	232.3 Da LogP 1.60 TPSA 68.1	✓ Ro5	✓ Clean	`CCOC(=O)[C@@H](N)Cc1c[nH]c2ccccc12`
ZINC53943847 ZINC	0.700	232.3 Da LogP 1.60 TPSA 68.1	✓ Ro5	✓ Clean	`CCOC(=O)[C@H](N)Cc1c[nH]c2ccccc12`
ZINC32189073 ZINC	0.692	220.2 Da LogP 0.83 TPSA 99.3	✓ Ro5	✓ Clean	`N[C@H](Cc1c[nH]c2cccc(O)c12)C(=O)O`
ZINC4240327 ZINC	0.692	218.3 Da LogP 1.51 TPSA 79.1	✓ Ro5	✓ Clean	`N[C@H](CC(=O)O)Cc1c[nH]c2ccccc12`
ZINC44544883 ZINC	0.692	218.3 Da LogP 1.37 TPSA 79.1	✓ Ro5	✓ Clean	`NC[C@H](Cc1c[nH]c2ccccc12)C(=O)O`
ZINC44544886 ZINC	0.692	218.3 Da LogP 1.37 TPSA 79.1	✓ Ro5	✓ Clean	`NC[C@@H](Cc1c[nH]c2ccccc12)C(=O)O`
ZINC4521117 ZINC	0.692	218.3 Da LogP 1.51 TPSA 79.1	✓ Ro5	✓ Clean	`N[C@@H](CC(=O)O)Cc1c[nH]c2ccccc12`
ZINC5843989 ZINC	0.692	220.2 Da LogP 0.83 TPSA 99.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]c2cccc(O)c12)C(=O)O`
ZINC178385 ZINC	0.684	203.2 Da LogP 2.43 TPSA 53.1	✓ Ro5	✓ Clean	`C[C@@H](Cc1c[nH]c2ccccc12)C(=O)O`
ZINC178387 ZINC	0.684	203.2 Da LogP 2.43 TPSA 53.1	✓ Ro5	✓ Clean	`C[C@H](Cc1c[nH]c2ccccc12)C(=O)O`
ZINC2539067 ZINC	0.682	333.4 Da LogP 3.19 TPSA 94.9	✓ Ro5	Alert	`N[C@@H](Cc1c(Cc2c[nH]c3ccccc23)[nH]c2ccccc12)C(…`
ZINC114287530 ZINC	0.675	330.1 Da LogP 1.73 TPSA 79.1	✓ Ro5	✓ Clean	`N[C@H](Cc1c[nH]c2ccc(I)cc12)C(=O)O`
ZINC14512177 ZINC	0.675	220.2 Da LogP 0.83 TPSA 99.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]c2cc(O)ccc12)C(=O)O`
ZINC14512180 ZINC	0.675	220.2 Da LogP 0.83 TPSA 99.3	✓ Ro5	✓ Clean	`N[C@H](Cc1c[nH]c2cc(O)ccc12)C(=O)O`
ZINC1691594 ZINC	0.675	219.2 Da LogP 0.70 TPSA 105.1	✓ Ro5	✓ Clean	`Nc1ccc2[nH]cc(C[C@H](N)C(=O)O)c2c1`
ZINC34279958 ZINC	0.675	330.1 Da LogP 1.73 TPSA 79.1	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]c2ccc(I)cc12)C(=O)O`
ZINC57131 ZINC	0.675	283.1 Da LogP 1.88 TPSA 79.1	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]c2ccc(Br)cc12)C(=O)O`
ZINC57132 ZINC	0.675	283.1 Da LogP 1.88 TPSA 79.1	✓ Ro5	✓ Clean	`N[C@H](Cc1c[nH]c2ccc(Br)cc12)C(=O)O`
ZINC6045354 ZINC	0.675	219.2 Da LogP 0.70 TPSA 105.1	✓ Ro5	✓ Clean	`Nc1ccc2[nH]cc(C[C@@H](N)C(=O)O)c2c1`
ZINC895330 ZINC	0.675	220.2 Da LogP 0.83 TPSA 99.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]c2ccc(O)cc12)C(=O)O`
ZINC895459 ZINC	0.675	220.2 Da LogP 0.83 TPSA 99.3	✓ Ro5	✓ Clean	`N[C@H](Cc1c[nH]c2ccc(O)cc12)C(=O)O`
ZINC20269567 ZINC	0.667	265.3 Da LogP 3.58 TPSA 53.1	✓ Ro5	✓ Clean	`O=C(O)[C@@H](Cc1c[nH]c2ccccc12)c1ccccc1`
ZINC20269568 ZINC	0.667	265.3 Da LogP 3.58 TPSA 53.1	✓ Ro5	✓ Clean	`O=C(O)[C@H](Cc1c[nH]c2ccccc12)c1ccccc1`
ZINC34402729 ZINC	0.667	204.2 Da LogP 1.12 TPSA 79.1	✓ Ro5	✓ Clean	`N[C@@H](Cc1cccc2[nH]ccc12)C(=O)O`
ZINC34402730 ZINC	0.667	204.2 Da LogP 1.12 TPSA 79.1	✓ Ro5	✓ Clean	`N[C@H](Cc1cccc2[nH]ccc12)C(=O)O`
ZINC34751367 ZINC	0.667	260.3 Da LogP 2.38 TPSA 68.1	✓ Ro5	✓ Clean	`CC(C)(C)OC(=O)[C@H](N)Cc1c[nH]c2ccccc12`
ZINC36468154 ZINC	0.667	244.3 Da LogP 1.77 TPSA 68.1	✓ Ro5	✓ Clean	`C=CCOC(=O)[C@@H](N)Cc1c[nH]c2ccccc12`
ZINC59313451 ZINC	0.667	260.3 Da LogP 2.38 TPSA 68.1	✓ Ro5	✓ Clean	`CC(C)(C)OC(=O)[C@@H](N)Cc1c[nH]c2ccccc12`
ZINC2516136 ZINC	0.659	283.1 Da LogP 1.88 TPSA 79.1	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]c2cc(Br)ccc12)C(=O)O`
ZINC2572392 ZINC	0.659	238.7 Da LogP 1.78 TPSA 79.1	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]c2ccc(Cl)cc12)C(=O)O`
ZINC391256 ZINC	0.659	218.3 Da LogP 1.43 TPSA 79.1	✓ Ro5	✓ Clean	`Cc1ccc2[nH]cc(C[C@H](N)C(=O)O)c2c1`
ZINC391257 ZINC	0.659	218.3 Da LogP 1.43 TPSA 79.1	✓ Ro5	✓ Clean	`Cc1ccc2[nH]cc(C[C@@H](N)C(=O)O)c2c1`
ZINC391258 ZINC	0.659	218.3 Da LogP 1.43 TPSA 79.1	✓ Ro5	✓ Clean	`Cc1ccc2c(C[C@H](N)C(=O)O)c[nH]c2c1`
ZINC391781 ZINC	0.659	218.3 Da LogP 1.43 TPSA 79.1	✓ Ro5	✓ Clean	`Cc1ccc2c(C[C@@H](N)C(=O)O)c[nH]c2c1`
ZINC56393 ZINC	0.659	222.2 Da LogP 1.26 TPSA 79.1	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]c2cc(F)ccc12)C(=O)O`
ZINC57156 ZINC	0.659	222.2 Da LogP 1.26 TPSA 79.1	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]c2ccc(F)cc12)C(=O)O`
ZINC57157 ZINC	0.659	222.2 Da LogP 1.26 TPSA 79.1	✓ Ro5	✓ Clean	`N[C@H](Cc1c[nH]c2ccc(F)cc12)C(=O)O`
ZINC9915769 ZINC	0.659	238.7 Da LogP 1.78 TPSA 79.1	✓ Ro5	✓ Clean	`N[C@H](Cc1c[nH]c2ccc(Cl)cc12)C(=O)O`

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.

Cross-references

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

Sequence

UniProt A0A0H3GZT5

Chemistry

ChEMBL DWT ChEMBL CHEMBL5070123 ChEMBL CHEMBL5079973 ChEMBL CHEMBL5092803 ChEMBL CHEMBL5284556