KpATCC43816 Protein target profile

tyrA

Accession: VK055_4578

Gene: AIK83116.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A0H3GRW1

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Length 373

Pocket druggability (P2Rank · AlphaFold DB model) 0.57

Direct ligand evidence 0 52 total records

Functional annotation 0 EC 7 GO

Target summary

Strong target candidate with converging metabolic, structural and chemical evidence.

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 0.57, FPocket 0.84). Use the 3D pocket comparison to verify whether they identify the same site. No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. 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. Review the complete evidence below

Risks to review

Evidence coverage

Core evidence streams are available for this target.

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: 3.0% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 41.935 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 94.23 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) 0.57

Structure A0A0H3GRW1

Pocket Pocket 1

Druggability (FPocket) 0.844

Structure A0A0H3GRW1

Pocket Pocket 13

ColabFold model

P2Rank 0.677 · Pocket 1

FPocket 0.867 · Pocket 37

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 141 / 4744 genomes with a hit

Prevalence 3.0%

Metabolic context

Reactions catalyzed, pathway membership, and centrality in the genome-scale metabolic network.

This protein is not associated with the imported metabolic network for this genome.

Browse the genome's metabolic network

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MVAELTALRDQIDEVDKALLSLLAKRLELVAEVGEVKSQYGLPIYVPERESAMLASRRKEAAALGVPPDLIEDVLRRVMRESYSSENDKGFKTLQPNLRPVVIVGGGGQMGRLFEKMLTLSGYQVRILEKEDWARAADIVADAGMVIVSVPIHTTVETIARLPPLPADCILVDLASVKAEPLQAMLAAHQGPVLGLHPMFGPDSGSLAKQVVVYCDGRQPEAYQWFLEQIQVWGARLHRISAVEHDQNMAFIQALRHFATFAYGLHLAEENVRLEQLLALSSPIYRLELAMVGRLFAQDPQLYADIIMSSENNLALIKRYYQRFGEAIGLLEQGDKQAFIDSFRKVEHWFGDYAQRFQSESRTLLRQANDNRQ

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

7 GO

Subcellular localization

Localization: Cytoplasmic

Gene Ontology (GO)

GO:0004665 Catalysis of the reaction: NADP+ + prephenate = (4-hydroxyphenyl)pyruvate + CO2 + NADPH.
GO:0004106 Catalysis of the reaction: chorismate = prephenate.
GO:0046417 The chemical reactions and pathways involving chorismate, the anion of (3R-trans)-3-((1-carboxyethenyl)oxy)-4-hydroxy-1,5-cyclohexadiene-1-carboxylic acid.
GO:0006571 The chemical reactions and pathways resulting in the formation of tyrosine, an aromatic amino acid, 2-amino-3-(4-hydroxyphenyl)propanoic acid.
GO:0070403 Binding to the oxidized form, NAD, of nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0008977 Catalysis of the reaction: NAD+ + prephenate = (4-hydroxyphenyl)pyruvate + CO2 + NADH.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

30 records

Show feature table

Start	End	DB	Term	Name
137	219	Pfam	PF02153	Prephenate dehydrogenase, nucleotide-binding domain
137	219	InterPro	IPR046826	Prephenate dehydrogenase, nucleotide-binding domain
5	87	NCBIfam	TIGR01799	chorismate mutase
5	87	InterPro	IPR011277	Chorismate mutase, T-protein
1	373	PIRSF	PIRSF001499	Chor_mut_pdh_Tpr
1	373	InterPro	IPR008244	Bifunctional chorismate mutase/prephenate dehydrogenase T-protein
91	238	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
91	238	InterPro	IPR036291	NAD(P)-binding domain superfamily
241	366	SUPERFAMILY	SSF48179	6-phosphogluconate dehydrogenase C-terminal domain-like
241	366	InterPro	IPR008927	6-phosphogluconate dehydrogenase-like, C-terminal domain superfamily
2	81	FunFam	G3DSA:1.20.59.10:FF:000001	T-protein
9	86	Pfam	PF01817	Chorismate mutase type II
9	86	InterPro	IPR002701	Chorismate mutase II, prokaryotic-type
9	89	SMART	SM00830	CM_2_4
9	89	InterPro	IPR002701	Chorismate mutase II, prokaryotic-type
99	361	ProSiteProfiles	PS51176	Prephenate/arogenate dehydrogenase domain profile.
99	361	InterPro	IPR003099	Prephenate dehydrogenase
2	81	Gene3D	G3DSA:1.20.59.10	Chorismate mutase
2	81	InterPro	IPR036979	Chorismate mutase domain superfamily
248	373	Gene3D	G3DSA:1.10.3660.10	-
1	90	ProSiteProfiles	PS51168	Chorismate mutase domain profile.
1	90	InterPro	IPR002701	Chorismate mutase II, prokaryotic-type
96	372	PANTHER	PTHR21363	PREPHENATE DEHYDROGENASE
4	88	SUPERFAMILY	SSF48600	Chorismate mutase II
4	88	InterPro	IPR036263	Chorismate mutase type II superfamily
82	246	Gene3D	G3DSA:3.40.50.720	-
243	344	Pfam	PF20463	Prephenate dehydrogenase, dimerization domain
243	344	InterPro	IPR046825	Prephenate dehydrogenase, dimerization domain
248	373	FunFam	G3DSA:1.10.3660.10:FF:000001	T-protein
82	246	FunFam	G3DSA:3.40.50.720:FF:000170	T-protein

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

0.57

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Surrounding area

Pocket 2 P2Rank #2

0.241

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Surrounding area

Pocket 3 P2Rank #3

0.045

Likely same site as FPocket 13 1.8 Å 7 shared residues 100% of smaller site

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Surrounding area

Pocket 4 P2Rank #4

0.033

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Surrounding area

Pocket 5 P2Rank #5

0.027

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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 #13

0.844

Likely same site as P2Rank 3 1.8 Å 7 shared residues 100% of smaller site

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Surrounding area

Pocket 2 FPocket #34

0.393

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Surrounding area

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.677

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Surrounding area

Pocket 2 P2Rank #2

0.214

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Surrounding area

Pocket 3 P2Rank #3

0.053

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Surrounding area

Pocket 4 P2Rank #4

0.014

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Surrounding area

Pocket 5 P2Rank #5

0.012

Likely same site as FPocket 37 1.8 Å 7 shared residues 100% of smaller site

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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 #37

0.867

Likely same site as P2Rank 5 1.8 Å 7 shared residues 100% of smaller site

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Surrounding area

Pocket 2 FPocket #41

0.204

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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_A0A0H3GRW1	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_4578	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.

52 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 2 records from similar proteins

Structural ligands 2 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

MLT PDB via homolog 134.1 Da · LogP -1.09 · TPSA 94.8 Open detail RCSB PDB

TSA PDB via homolog Detail RCSB PDB

ZINC403598 ZINC proposed compound · Tanimoto 0.800 Detail ZINC

ZINC403599 ZINC proposed compound · Tanimoto 0.800 Detail ZINC

ZINC39351856 ZINC proposed compound · Tanimoto 0.741 Detail ZINC

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
MLT RCSB PDB	3RMI	A0A0H3LYP5	134.1 Da LogP -1.09 TPSA 94.8	✓ Ro5	✓ Clean	`C([C@H](C(=O)O)O)C(=O)O`
TSA RCSB PDB	2GTV	Q57696	228.2 Da LogP -0.38 TPSA 104.1	✓ Ro5	✓ Clean	`C1[C@@H]2[C@@H](C=C[C@]1(C[C@H](O2)C(=O)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).

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
ZINC403598 ZINC	0.800	273.3 Da LogP 2.14 TPSA 92.8	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(Oc2ccc(O)cc2)cc1)C(=O)O`
ZINC403599 ZINC	0.800	273.3 Da LogP 2.14 TPSA 92.8	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(Oc2ccc(O)cc2)cc1)C(=O)O`
ZINC39351856 ZINC	0.741	328.4 Da LogP 1.26 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(-c2ccc(C[C@H](N)C(=O)O)cc2)cc1)C…`
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`
ZINC32333 ZINC	0.690	244.1 Da LogP 1.40 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(Br)cc1)C(=O)O`
ZINC32334 ZINC	0.690	244.1 Da LogP 1.40 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(Br)cc1)C(=O)O`
ZINC3679925 ZINC	0.690	291.1 Da LogP 1.25 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(I)cc1)C(=O)O`
ZINC391104 ZINC	0.690	291.1 Da LogP 1.25 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(I)cc1)C(=O)O`
ZINC4202286 ZINC	0.690	209.2 Da LogP 0.34 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(C(=O)O)cc1)C(=O)O`
ZINC4202287 ZINC	0.690	209.2 Da LogP 0.34 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(C(=O)O)cc1)C(=O)O`
ZINC6092920 ZINC	0.690	223.2 Da LogP 0.27 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(CC(=O)O)cc1)C(=O)O`
ZINC6506146 ZINC	0.690	223.2 Da LogP 0.27 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(CC(=O)O)cc1)C(=O)O`
ZINC34319489 ZINC	0.688	231.3 Da LogP 1.50 TPSA 83.5	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc2cc(O)ccc2c1)C(=O)O`
ZINC34319490 ZINC	0.688	231.3 Da LogP 1.50 TPSA 83.5	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc2cc(O)ccc2c1)C(=O)O`
ZINC2512061 ZINC	0.677	360.4 Da LogP 0.67 TPSA 167.1	1 viol.	✓ Clean	`N[C@@H](Cc1ccc(O)c(-c2cc(C[C@H](N)C(=O)O)ccc2O)…`
ZINC6091882 ZINC	0.677	360.4 Da LogP 0.67 TPSA 167.1	1 viol.	✓ Clean	`N[C@@H](Cc1ccc(O)c(-c2cc(C[C@@H](N)C(=O)O)ccc2O…`
ZINC6091894 ZINC	0.677	360.4 Da LogP 0.67 TPSA 167.1	1 viol.	✓ Clean	`N[C@H](Cc1ccc(O)c(-c2cc(C[C@@H](N)C(=O)O)ccc2O)…`
ZINC113264413 ZINC	0.667	317.4 Da LogP 3.98 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(-c2ccc(-c3ccccc3)cc2)cc1)C(=O)O`
ZINC113264415 ZINC	0.667	317.4 Da LogP 3.98 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(-c2ccc(-c3ccccc3)cc2)cc1)C(=O)O`
ZINC14982778 ZINC	0.667	207.2 Da LogP 0.84 TPSA 80.4	✓ Ro5	✓ Clean	`CC(=O)c1ccc(C[C@@H](N)C(=O)O)cc1`
ZINC14982780 ZINC	0.667	207.2 Da LogP 0.84 TPSA 80.4	✓ Ro5	✓ Clean	`CC(=O)c1ccc(C[C@H](N)C(=O)O)cc1`
ZINC1569734 ZINC	0.667	238.2 Da LogP -0.54 TPSA 112.6	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(O)cc1)C(=O)NCC(=O)O`
ZINC2244337 ZINC	0.667	241.3 Da LogP 2.31 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(-c2ccccc2)cc1)C(=O)O`
ZINC2244338 ZINC	0.667	241.3 Da LogP 2.31 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(-c2ccccc2)cc1)C(=O)O`
ZINC2505456 ZINC	0.667	210.2 Da LogP 0.72 TPSA 94.8	✓ Ro5	✓ Clean	`O=C(O)C(Cc1ccc(O)cc1)C(=O)O`
ZINC2575475 ZINC	0.667	238.2 Da LogP -0.54 TPSA 112.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(O)cc1)C(=O)NCC(=O)O`
ZINC2575618 ZINC	0.667	208.2 Da LogP -0.26 TPSA 106.4	✓ Ro5	✓ Clean	`NC(=O)c1ccc(C[C@H](N)C(=O)O)cc1`
ZINC4241956 ZINC	0.667	208.2 Da LogP -0.26 TPSA 106.4	✓ Ro5	✓ Clean	`NC(=O)c1ccc(C[C@@H](N)C(=O)O)cc1`
ZINC71773889 ZINC	0.667	206.1 Da LogP -1.77 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(C[C@H](O)C(=O)O)C[C@H](O)C(=O)O`
ZINC71773890 ZINC	0.667	206.1 Da LogP -1.77 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(C[C@H](O)C(=O)O)C[C@@H](O)C(=O)O`
ZINC71773891 ZINC	0.667	206.1 Da LogP -1.77 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(C[C@@H](O)C(=O)O)C[C@@H](O)C(=O)O`
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`
ZINC2004481 ZINC	0.647	344.4 Da LogP 0.78 TPSA 132.9	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](Cc1ccc(O)cc1)…`
ZINC116924508 ZINC	0.645	215.2 Da LogP 1.58 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(C(F)F)cc1)C(=O)O`
ZINC116924543 ZINC	0.645	215.2 Da LogP 1.58 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(C(F)F)cc1)C(=O)O`
ZINC2385595 ZINC	0.645	207.3 Da LogP 1.76 TPSA 63.3	✓ Ro5	✓ Clean	`CC(C)c1ccc(C[C@H](N)C(=O)O)cc1`
ZINC2392305 ZINC	0.645	221.3 Da LogP 1.94 TPSA 63.3	✓ Ro5	✓ Clean	`CC(C)(C)c1ccc(C[C@H](N)C(=O)O)cc1`
ZINC2392306 ZINC	0.645	221.3 Da LogP 1.94 TPSA 63.3	✓ Ro5	✓ Clean	`CC(C)(C)c1ccc(C[C@@H](N)C(=O)O)cc1`
ZINC3679865 ZINC	0.645	207.3 Da LogP 1.76 TPSA 63.3	✓ Ro5	✓ Clean	`CC(C)c1ccc(C[C@@H](N)C(=O)O)cc1`
ZINC44283754 ZINC	0.645	207.3 Da LogP 1.59 TPSA 63.3	✓ Ro5	✓ Clean	`CCCc1ccc(C[C@H](N)C(=O)O)cc1`
ZINC44283756 ZINC	0.645	207.3 Da LogP 1.59 TPSA 63.3	✓ Ro5	✓ Clean	`CCCc1ccc(C[C@@H](N)C(=O)O)cc1`
ZINC44284738 ZINC	0.645	255.3 Da LogP 2.62 TPSA 63.3	✓ Ro5	✓ Clean	`Cc1ccc(-c2ccc(C[C@H](N)C(=O)O)cc2)cc1`
ZINC44284740 ZINC	0.645	255.3 Da LogP 2.62 TPSA 63.3	✓ Ro5	✓ Clean	`Cc1ccc(-c2ccc(C[C@@H](N)C(=O)O)cc2)cc1`
ZINC4763192 ZINC	0.636	271.3 Da LogP 2.01 TPSA 72.5	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(O)cc1)C(=O)OCc1ccccc1`
ZINC4763195 ZINC	0.636	271.3 Da LogP 2.01 TPSA 72.5	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(O)cc1)C(=O)OCc1ccccc1`
ZINC2566273 ZINC	0.629	252.3 Da LogP -0.15 TPSA 112.7	✓ Ro5	✓ Clean	`C[C@H](NC(=O)[C@@H](N)Cc1ccc(O)cc1)C(=O)O`
ZINC3590784 ZINC	0.629	252.3 Da LogP -0.15 TPSA 112.7	✓ Ro5	✓ Clean	`C[C@@H](NC(=O)[C@@H](N)Cc1ccc(O)cc1)C(=O)O`
ZINC4787311 ZINC	0.629	252.3 Da LogP -0.15 TPSA 112.7	✓ Ro5	✓ Clean	`C[C@H](NC(=O)[C@H](N)Cc1ccc(O)cc1)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 A0A0H3GRW1