KpATCC43816 Protein target profile

3-deoxy-7-phosphoheptulonate synthase

Accession: VK055_4577

Gene: AIK83115.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism 1 reaction UniProt A0A0H3GWX1

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Length 356

Pocket druggability (P2Rank · AlphaFold DB model) 0.583

Metabolic reactions 1

Chokepoint Yes

Direct ligand evidence 0 58 total records

Functional annotation 1 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

Metabolic chokepoint Catalyzes a reaction that is the only producer or consumer of a metabolite in the imported metabolic model. Central metabolic position More central than 95.6% of genes in this genome. 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. 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: 5.1% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 52.326 Higher values support similarity to known essential genes.
DEG E-value: 3.28e-136 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 96.79 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) 0.583

Structure A0A0H3GWX1

Pocket Pocket 1

Druggability (FPocket) 0.669

Structure A0A0H3GWX1

Pocket Pocket 1

ColabFold model

P2Rank 0.5 · Pocket 1

FPocket 0.624 · Pocket 3

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 243 / 4744 genomes with a hit

Prevalence 5.1%

Metabolic context

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

Explore metabolic network

Attractive metabolic target: catalyzes a producing chokepoint reaction in Phenylalanine, tyrosine and tryptophan biosynthesis, more central than 95.6% of genes in this genome, no human homolog detected.

Relative network centrality 95.6% more central than 95.6% of genes in this genome

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MQKDALNNVHITDEHVLMTPEQLKAEFPLSVEQEAQIAHARQTISDIIAGRDPRLLVVCGPCSIHDPEAAIEYARRFKALAAEVSDSLYLVMRVYFEKPRTTVGWKGLINDPHMDGSFDVEGGLKIARRLLVELVNMGLPLATEALDPNSPQYLGDLFSWSAIGARTTESQTHREMASGLSMPVGFKNGTDGSLATAINAMRAAAMPHRFVGINQAGQVCLLQTQGNPNGHVILRGGKAPNYGPEDVAKCEKEMAQAGLKPSLMVDCSHGNSNKDFRRQPAVAESVVAQIKDGNRSIIGLMIESNIHEGNQSSEQPREAMKYGVSVTDACISWETTEALLRELDKDLRGHLAARLV

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

2.5.1.54

Gene Ontology (GO)

GO:0009073 The chemical reactions and pathways resulting in the formation of aromatic amino acid family, amino acids with aromatic ring (phenylalanine, tyrosine, tryptophan).
GO:0003849 Catalysis of the reaction: D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate.
GO:0009058 A cellular process consisting of the biochemical pathways by which a living organism synthesizes chemical substances. This typically represents the energy-requiring part of metabolism in which simpler substances are transformed into more complex ones.
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:0008652 The chemical reactions and pathways resulting in the formation of amino acids, organic acids containing one or more amino substituents.
GO:0009423 The chemical reactions and pathways resulting in the formation of the unsymmetrical ether derived from phosphoenolpyruvate and 5-phosphoshikimic acid formed as an intermediate in the biosynthesis of aromatic amino acids and many other compounds.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

12 records

Show feature table

Start	End	DB	Term	Name
9	349	NCBIfam	TIGR00034	3-deoxy-7-phosphoheptulonate synthase
9	349	InterPro	IPR006219	DAHP synthase, class 1
8	345	SUPERFAMILY	SSF51569	Aldolase
1	353	Gene3D	G3DSA:3.20.20.70	Aldolase class I
1	353	InterPro	IPR013785	Aldolase-type TIM barrel
1	354	FunFam	G3DSA:3.20.20.70:FF:000005	Phospho-2-dehydro-3-deoxyheptonate aldolase
2	349	PANTHER	PTHR21225	PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE DAHP SYNTHETASE
2	349	InterPro	IPR006219	DAHP synthase, class 1
38	340	Pfam	PF00793	DAHP synthetase I family
38	340	InterPro	IPR006218	DAHP synthetase I/KDSA
1	354	PIRSF	PIRSF001361	DAHP_synthase
1	354	InterPro	IPR006219	DAHP synthase, class 1

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

0.583

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Surrounding area

Pocket 2 P2Rank #2

0.183

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Surrounding area

Pocket 3 P2Rank #3

0.16

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Surrounding area

Pocket 4 P2Rank #4

0.039

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Surrounding area

Pocket 5 P2Rank #5

0.028

Likely same site as FPocket 1 1.0 Å 11 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 #1

0.669

Likely same site as P2Rank 5 1.0 Å 11 shared residues 100% of smaller site

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

0.5

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Surrounding area

Pocket 2 P2Rank #2

0.364

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Surrounding area

Pocket 3 P2Rank #3

0.047

Likely same site as FPocket 18 4.0 Å 10 shared residues 100% of smaller site

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Surrounding area

Pocket 4 P2Rank #4

0.022

Likely same site as FPocket 3 1.0 Å 9 shared residues 100% of smaller site

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Surrounding area

Pocket 5 P2Rank #5

0.015

Likely same site as FPocket 3 7.4 Å 4 shared residues 57% 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 #3

0.624

Likely same site as P2Rank 4 1.0 Å 9 shared residues 100% of smaller site

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Surrounding area

Pocket 2 FPocket #18

0.232

Likely same site as P2Rank 3 4.0 Å 10 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_A0A0H3GWX1	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_4577	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

0V5 PDB via homolog 170.1 Da · LogP -0.43 · TPSA 104.1 Open detail RCSB PDB

DTY PDB via homolog Detail RCSB PDB

G3P PDB via homolog Detail RCSB PDB

GZ3 PDB via homolog Detail RCSB PDB

PEP 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
0V5 RCSB PDB	4UMB	Q9K169	170.1 Da LogP -0.43 TPSA 104.1	✓ Ro5	✓ Clean	`C[C@H](C(=O)O)OP(=O)(O)O`
DTY RCSB PDB	1OF6	P32449	181.2 Da LogP 0.35 TPSA 83.5	✓ Ro5	✓ Clean	`c1cc(ccc1C[C@H](C(=O)O)N)O`
G3P RCSB PDB	1OF8	P32449	172.1 Da LogP -1.55 TPSA 107.2	✓ Ro5	✓ Clean	`C([C@H](COP(=O)(O)O)O)O`
GZ3 RCSB PDB	4UMA	Q9K169	166.1 Da LogP 0.15 TPSA 94.8	✓ Ro5	✓ Clean	`C/C(=C\P(=O)(O)O)/C(=O)O`
PEP RCSB PDB	4HSN	Q9K169	168.0 Da LogP -0.31 TPSA 104.1	✓ Ro5	✓ Clean	`C=C(C(=O)O)OP(=O)(O)O`
PEQ RCSB PDB	4UMC	Q9K169	170.1 Da LogP -0.43 TPSA 104.1	✓ Ro5	✓ Clean	`C[C@@H](C(=O)O)OP(=O)(O)O`
PGA RCSB PDB	1GG1	P0AB91	156.0 Da LogP -0.82 TPSA 104.1	✓ Ro5	✓ Clean	`C(C(=O)O)OP(=O)(O)O`
TMO RCSB PDB	5D09	Q9K169	75.1 Da LogP 0.19 TPSA 23.1	✓ Ro5	✓ Clean	`C[N+](C)(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
ZINC83315 ZINC	1.000	204.2 Da LogP 1.12 TPSA 79.1	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]c2ccccc12)C(=O)O`
ZINC83317 ZINC	1.000	204.2 Da LogP 1.12 TPSA 79.1	✓ Ro5	✓ Clean	`N[C@H](Cc1c[nH]c2ccccc12)C(=O)O`
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`
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`
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…`
ZINC1637998 ZINC	0.732	261.3 Da LogP 0.24 TPSA 108.2	✓ Ro5	✓ Clean	`N[C@H](Cc1c[nH]c2ccccc12)C(=O)NCC(=O)O`
ZINC2384992 ZINC	0.732	261.3 Da LogP 0.24 TPSA 108.2	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]c2ccccc12)C(=O)NCC(=O)O`
ZINC264238 ZINC	0.732	293.4 Da LogP 2.35 TPSA 70.9	✓ Ro5	✓ Clean	`N[C@H](Cc1c[nH]c2ccccc12)C(=O)NCc1ccccc1`
ZINC264242 ZINC	0.732	293.4 Da LogP 2.35 TPSA 70.9	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]c2ccccc12)C(=O)NCc1ccccc1`
ZINC34781219 ZINC	0.718	218.3 Da LogP 1.21 TPSA 68.1	✓ Ro5	✓ Clean	`COC(=O)[C@H](N)Cc1c[nH]c2ccccc12`
ZINC34781220 ZINC	0.718	218.3 Da LogP 1.21 TPSA 68.1	✓ Ro5	✓ Clean	`COC(=O)[C@@H](N)Cc1c[nH]c2ccccc12`
ZINC1557161 ZINC	0.714	390.4 Da LogP 2.33 TPSA 124.0	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@@H](Cc1c[nH]…`
ZINC1557164 ZINC	0.714	390.4 Da LogP 2.33 TPSA 124.0	✓ Ro5	✓ Clean	`N[C@H](Cc1c[nH]c2ccccc12)C(=O)N[C@H](Cc1c[nH]c2…`
ZINC193616 ZINC	0.707	279.3 Da LogP 2.68 TPSA 70.9	✓ Ro5	✓ Clean	`N[C@H](Cc1c[nH]c2ccccc12)C(=O)Nc1ccccc1`
ZINC2497690 ZINC	0.707	279.3 Da LogP 2.68 TPSA 70.9	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]c2ccccc12)C(=O)Nc1ccccc1`
ZINC874230 ZINC	0.707	231.3 Da LogP 1.17 TPSA 70.9	✓ Ro5	✓ Clean	`CCNC(=O)[C@H](N)Cc1c[nH]c2ccccc12`
ZINC874233 ZINC	0.707	231.3 Da LogP 1.17 TPSA 70.9	✓ Ro5	✓ Clean	`CCNC(=O)[C@@H](N)Cc1c[nH]c2ccccc12`
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`
ZINC34307123 ZINC	0.700	217.3 Da LogP 0.78 TPSA 70.9	✓ Ro5	✓ Clean	`CNC(=O)[C@@H](N)Cc1c[nH]c2ccccc12`
ZINC34482181 ZINC	0.700	217.3 Da LogP 0.78 TPSA 70.9	✓ Ro5	✓ Clean	`CNC(=O)[C@H](N)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`
ZINC1638007 ZINC	0.698	275.3 Da LogP 0.63 TPSA 108.2	✓ Ro5	✓ Clean	`C[C@H](NC(=O)[C@@H](N)Cc1c[nH]c2ccccc12)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`
ZINC2134508 ZINC	0.690	245.3 Da LogP 1.56 TPSA 70.9	✓ Ro5	✓ Clean	`CCCNC(=O)[C@H](N)Cc1c[nH]c2ccccc12`
ZINC2134510 ZINC	0.690	245.3 Da LogP 1.56 TPSA 70.9	✓ Ro5	✓ Clean	`CCCNC(=O)[C@@H](N)Cc1c[nH]c2ccccc12`
ZINC2559489 ZINC	0.690	260.3 Da LogP -0.36 TPSA 114.0	✓ Ro5	✓ Clean	`NC(=O)CNC(=O)[C@@H](N)Cc1c[nH]c2ccccc12`
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`
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`
ZINC83138985 ZINC	0.684	223.7 Da LogP 2.40 TPSA 53.1	✓ Ro5	✓ Clean	`O=C(O)[C@@H](Cl)Cc1c[nH]c2ccccc12`

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 A0A0H3GWX1

Pathways

KEGG R01826 BioCyc DAHPSYN-RXN