KpATCC43816 Protein target profile

aminodeoxychorismate synthase, component I

Accession: VK055_0122

Gene: pabB AIK78750.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism 3 reactions UniProt A0A0H3GZZ4

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Length 451

Pocket druggability (P2Rank · AlphaFold DB model) 0.942

Metabolic reactions 3

Chokepoint No

Direct ligand evidence 0 56 total records

Functional annotation 1 EC 6 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

Central metabolic position More central than 90.2% 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. Second pocket predictor agrees P2Rank predicted binding-site probability 0.94. 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: 2.6% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 78.667 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 94.58 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) 0.942

Structure A0A0H3GZZ4

Pocket Pocket 1

Druggability (FPocket) 0.82

Structure A0A0H3GZZ4

Pocket Pocket 1

ColabFold model

P2Rank 0.949 · Pocket 1

FPocket 0.705 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 121 / 4744 genomes with a hit

Prevalence 2.6%

Metabolic context

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

Explore metabolic network

Metabolic context: more central than 90.2% of genes in this genome, no human homolog detected.

Relative network centrality 90.2% more central than 90.2% of genes in this genome

Chokepoint Not a chokepoint

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MLSPAIITLPWRPDAAEHYFAPLSALPWAMLLHSGFADHPHNRFDILVAAPRATLLTRGEQTWVDDGETVVVSAEDPLQLLQQQLDRQPFTPQPHDDLPFLGGALGLFGYDLGRRFERLPSHAQADIALADMAVGIYDWALIVDHQRQQISLLSYDDPQRRFQWLLAQSSPAMKPFALTSAWQSNMSRQQYGEKFRQVQAYLHSGDCYQVNLAQRFQASYVGDEWLAFRQLNAVNRAPFSAFIRLDEGAILSLSPERFIQLRQGEIQTRPIKGTLPRLDSPLADAQQAEKLANSPKDRAENLMIVDLMRNDIGRVAVPGSVRVPELFVVEPFPAVHHLVSTITARLPMTLHASDLLRAAFPGGSITGAPKVRAMEIIDELEPQRRNAWCGSIGYLSYCGNMDTSITIRTLTAWQGQLYCSAGGGIVADSEEAAEYQETFDKVNRILQQLEN

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

2.6.1.85

Gene Ontology (GO)

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:0009396 The chemical reactions and pathways resulting in the formation of folic acid and its derivatives.
GO:0046820 Catalysis of the reaction: L-glutamine + chorismate = 4-amino-4-deoxychorismate + L-glutamate. It is composed of two enzymatic activities (which may be present on one or two polypeptides); the first is a glutaminase which yields ammonia from glutamine, releasing glutamate. The ammonia is used by the second activity which catalyzes the amination of chorismate to form 4-amino-4-deoxychorismate.
GO:0046656 The chemical reactions and pathways resulting in the formation of folic acid, pteroylglutamic acid.
GO:0000162 The chemical reactions and pathways resulting in the formation of L-tryptophan, the chiral amino acid 2-amino-3-(1H-indol-3-yl)propanoic acid; L-tryptophan is synthesized from chorismate via anthranilate.
GO:0046654 The chemical reactions and pathways resulting in the formation of tetrahydrofolate, 5,6,7,8-tetrahydrofolic acid, a folate derivative bearing additional hydrogens on the pterin group.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

22 records

Show feature table

Start	End	DB	Term	Name
1	451	FunFam	G3DSA:3.60.120.10:FF:000004	Aminodeoxychorismate synthase, component I
20	150	Pfam	PF04715	Anthranilate synthase component I, N terminal region
20	150	InterPro	IPR006805	Anthranilate synthase component I, N-terminal
105	445	NCBIfam	TIGR00553	aminodeoxychorismate synthase component I
105	445	InterPro	IPR005802	Aminodeoxychorismate synthase, component I
4	449	SUPERFAMILY	SSF56322	ADC synthase
4	449	InterPro	IPR005801	ADC synthase
30	448	PANTHER	PTHR11236	AMINOBENZOATE/ANTHRANILATE SYNTHASE
30	448	InterPro	IPR019999	Anthranilate synthase component I-like
398	412	PRINTS	PR00095	Anthranilate synthase component I signature
398	412	InterPro	IPR019999	Anthranilate synthase component I-like
289	302	PRINTS	PR00095	Anthranilate synthase component I signature
289	302	InterPro	IPR019999	Anthranilate synthase component I-like
383	397	PRINTS	PR00095	Anthranilate synthase component I signature
383	397	InterPro	IPR019999	Anthranilate synthase component I-like
303	316	PRINTS	PR00095	Anthranilate synthase component I signature
303	316	InterPro	IPR019999	Anthranilate synthase component I-like
432	451	Coils	Coil	Coil
188	441	Pfam	PF00425	chorismate binding enzyme
188	441	InterPro	IPR015890	Chorismate-utilising enzyme, C-terminal
1	451	Gene3D	G3DSA:3.60.120.10	Anthranilate synthase
1	451	InterPro	IPR005801	ADC synthase

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

0.942

Likely same site as FPocket 29 2.4 Å 33 shared residues 94% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.452

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Surrounding area

Pocket 3 P2Rank #3

0.355

Likely same site as FPocket 1 2.0 Å 16 shared residues 100% of smaller site

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Surrounding area

Pocket 4 P2Rank #4

0.113

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Surrounding area

Pocket 5 P2Rank #5

0.013

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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

0.82 Unusual size

Likely same site as P2Rank 3 2.0 Å 16 shared residues 100% of smaller site

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Surrounding area

Pocket 2 FPocket #29

0.423 Unusual size

Likely same site as P2Rank 1 2.4 Å 33 shared residues 94% of smaller site

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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

0.949

Likely same site as FPocket 25 2.3 Å 33 shared residues 87% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.423

Likely same site as FPocket 1 1.7 Å 20 shared residues 100% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.334

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Surrounding area

Pocket 4 P2Rank #4

0.042

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Surrounding area

Pocket 5 P2Rank #5

0.009

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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

0.705 Unusual size

Likely same site as P2Rank 2 1.7 Å 20 shared residues 100% of smaller site

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Surrounding area

Pocket 2 FPocket #25

0.498 Unusual size

Likely same site as P2Rank 1 2.3 Å 33 shared residues 87% of smaller site

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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_A0A0H3GZZ4	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_0122	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.

56 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 6 records from similar proteins

Structural ligands 5 0 loaded crystals

Measured bioactivity 1 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

0GA PDB via homolog 238.2 Da · LogP 1.46 · TPSA 104.1 Open detail RCSB PDB

15P PDB via homolog Detail RCSB PDB

BEZ PDB via homolog Detail RCSB PDB

CPS PDB via homolog Detail RCSB PDB

PYR 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
0GA RCSB PDB	5CWA	P9WFX2	238.2 Da LogP 1.46 TPSA 104.1	✓ Ro5	✓ Clean	`C/C=C(/C(=O)O)\Oc1cccc(c1O)C(=O)O`
15P RCSB PDB	4GRH	B2FR92	1529.8 Da LogP 0.17 TPSA 334.1	2 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO…`
BEZ RCSB PDB	7BVD	A0QX93	122.1 Da LogP 1.38 TPSA 37.3	✓ Ro5	✓ Clean	`c1ccc(cc1)C(=O)O`
CPS RCSB PDB	4GRH	B2FR92	614.9 Da LogP 2.88 TPSA 147.0	1 viol.	✓ Clean	`C[C@H](CCC(=O)NCCC[N+](C)(C)CCCS(=O)(=O)[O-])[C…`
PYR RCSB PDB	7BVD	A0QX93	88.1 Da LogP -0.34 TPSA 54.4	✓ Ro5	✓ Clean	`CC(=O)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
CHEMBL216545 ChEMBL	P00898	—	196.2 Da LogP 0.85 TPSA 83.8	✓ Ro5	✓ Clean	`O=C(O)COc1cccc(C(=O)O)c1`

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
ZINC1580161 ZINC	1.000	208.3 Da LogP -0.33 TPSA 57.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCO`
ZINC16052118 ZINC	1.000	340.4 Da LogP -0.28 TPSA 84.8	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCO`
ZINC16052257 ZINC	1.000	384.5 Da LogP -0.26 TPSA 94.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC34317654 ZINC	1.000	472.6 Da LogP -0.23 TPSA 112.5	1 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC44076059 ZINC	1.000	428.5 Da LogP -0.24 TPSA 103.3	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC5210101 ZINC	1.000	252.3 Da LogP -0.31 TPSA 66.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCO`
ZINC5997860 ZINC	1.000	296.4 Da LogP -0.29 TPSA 75.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCO`
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`
ZINC3269660 ZINC	0.824	254.2 Da LogP 2.45 TPSA 71.4	✓ Ro5	Alert	`O=C(O)c1ccc(C(=O)C(=O)c2ccccc2)cc1`
ZINC2504355 ZINC	0.778	226.2 Da LogP 2.62 TPSA 54.4	✓ Ro5	✓ Clean	`O=C(O)c1ccc(C(=O)c2ccccc2)cc1`
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`
ZINC332363 ZINC	0.750	226.2 Da LogP 0.61 TPSA 93.1	✓ Ro5	✓ Clean	`O=C(O)COc1cccc(OCC(=O)O)c1`
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`
ZINC72399572 ZINC	0.733	492.7 Da LogP 3.43 TPSA 93.0	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)NCCCN(C)C)[C@H]1CC[C@H]2[C@H]3[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`
ZINC575419714 ZINC	0.727	312.4 Da LogP 0.42 TPSA 66.4	✓ Ro5	✓ Clean	`COCCOCCOCCSCCOCCOCCO`
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…`
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`
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`
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`
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`
ZINC19504011 ZINC	0.706	210.2 Da LogP 0.94 TPSA 72.8	✓ Ro5	✓ Clean	`COC(=O)COc1cccc(C(=O)O)c1`
ZINC34161407 ZINC	0.706	210.2 Da LogP 0.94 TPSA 72.8	✓ Ro5	✓ Clean	`COC(=O)c1cccc(OCC(=O)O)c1`
ZINC1889002139 ZINC	0.703	449.7 Da LogP 3.89 TPSA 89.8	✓ Ro5	✓ Clean	`CCCNC(=O)CC[C@@H](C)[C@H]1CC[C@@H]2[C@H]3[C@H](…`
ZINC1889002140 ZINC	0.703	449.7 Da LogP 3.89 TPSA 89.8	✓ Ro5	✓ Clean	`CCCNC(=O)CC[C@@H](C)[C@H]1CC[C@@H]2[C@H]3[C@H](…`
ZINC1889002141 ZINC	0.703	449.7 Da LogP 3.89 TPSA 89.8	✓ Ro5	✓ Clean	`CCCNC(=O)CC[C@@H](C)[C@H]1CC[C@@H]2[C@@H]3[C@H]…`
ZINC1889002142 ZINC	0.703	449.7 Da LogP 3.89 TPSA 89.8	✓ Ro5	✓ Clean	`CCCNC(=O)CC[C@@H](C)[C@H]1CC[C@@H]2[C@@H]3[C@H]…`
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`
ZINC115163232 ZINC	0.700	222.3 Da LogP 0.07 TPSA 57.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCCO`
ZINC258837490 ZINC	0.700	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCCO`
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`

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.

aminodeoxychorismate synthase, component I

Promising target candidate with multiple supporting evidence streams.

Main supporting evidence

Risks to review

Evidence coverage

Prioritization evidence

Off-target risk

Essentiality

Structure confidence

Binding-site evidence

Metabolic context

Sequence

Functional annotations

Subcellular localization

Enzyme Commission (EC)

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · P2Rank

Binding pockets · FPocket

Binding pockets · P2Rank

Binding pockets · FPocket

Structural evidence

Ligand evidence

Cross-references

Sequence

Chemistry

Pathways