KpATCC43816 Protein target profile

arginine decarboxylase

Accession: VK055_4106

Gene: speA AIK82652.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism 2 reactions UniProt A0A0H3GT44

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Length 632

Pocket druggability (P2Rank · AlphaFold DB model) 0.886

Metabolic reactions 2

Chokepoint No

Direct ligand evidence 0 54 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

No isoenzyme backup detected Imported GPR rules do not show an alternative enzyme for the catalyzed reaction set. 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. Moderate predicted binding pocket FPocket selected-pocket score 0.64. This supports review but is not experimental 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: 2.8% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 44.462 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 92.61 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) 0.886

Structure A0A0H3GT44

Pocket Pocket 1

Druggability (FPocket) 0.639

Structure A0A0H3GT44

Pocket Pocket 9

ColabFold model

P2Rank 0.859 · Pocket 1

FPocket 0.757 · Pocket 2

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 132 / 4744 genomes with a hit

Prevalence 2.8%

Metabolic context

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

Explore metabolic network

Metabolic context: no human homolog detected.

Relative network centrality 0.0% more central than 0.0% of genes in this genome

Chokepoint Not a chokepoint

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MSSQEASKMLRTYNIAWWGNNYYDVNELGHISVCPDPDVPEARVDLAELVKAREAQGQRLPALFCFPQILQHRLRSINAAFKRARESYGYNGDYFLVYPIKVNQHRRVIESLIHSGEPLGLEAGSKAELMAVLAHAGMTRSVIVCNGYKDREYIRLALVGEKMGHKVYLVIEKMSEIAIVLEEAERLNVVPRLGVRARLASQGSGKWQSSGGEKSKFGLAATQVLQLVEILREAGHLESLQLLHFHLGSQMANIRDIATGVRESARFYVELHKLGVNIQCFDVGGGLGVDYEGTRSQSDCSVNYGLNEYANNIIWAIGDACEENGLPHPTVITESGRAVTAHHTVLVSNIIGVERNEYTEATPPAEDAARPLQSMWETWLEMHETGNRRSLREWLHDSQMDLHDIHIGYSSGTFNLQERAWAEQLYLNMCHEVQKQLDPSNRAHRPIIDELQERMADKIYVNFSLFQSMPDAWGIDQLFPVMPLEGLNKSPERRAVLLDITCDSDGAIDHYVDGDGIATTMPMPEYDPENPPMLGFFMVGAYQEILGNMHNLFGDTEAVDVFVFPDGSVEVELSDEGDTVADMLQYVQLDPNTLLTQFRDQVKNTGLDDALQQQFLEEFEAGLYGYTYLEDE

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Subcellular localization

Localization: Periplasmic

Enzyme Commission (EC)

4.1.1.19

Gene Ontology (GO)

GO:0008295 The chemical reactions and pathways resulting in the formation of spermidine, N-(3-aminopropyl)-1,4-diaminobutane.
GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
GO:0008792 Catalysis of the reaction: L-arginine + H+ = agmatine + CO2.
GO:0006527 The chemical reactions and pathways resulting in the breakdown of L-arginine.
GO:0046872 Binding to a metal ion.
GO:0033388 The chemical reactions and pathways resulting in the formation of putrescine, 1,4-diaminobutane, from other compounds, including arginine.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

62 records

Show feature table

Start	End	DB	Term	Name
74	341	Pfam	PF02784	Pyridoxal-dependent decarboxylase, pyridoxal binding domain
74	341	InterPro	IPR022644	Orn/DAP/Arg decarboxylase 2, N-terminal
455	558	SUPERFAMILY	SSF50621	Alanine racemase C-terminal domain-like
455	558	InterPro	IPR009006	Alanine racemase/group IV decarboxylase, C-terminal
4	631	PANTHER	PTHR43295	ARGININE DECARBOXYLASE
4	631	InterPro	IPR002985	Arginine decarboxylase
579	632	FunFam	G3DSA:1.10.287.3440:FF:000001	Biosynthetic arginine decarboxylase
487	512	PRINTS	PR01180	Arginine decarboxylase signature
487	512	InterPro	IPR002985	Arginine decarboxylase
90	104	PRINTS	PR01180	Arginine decarboxylase signature
90	104	InterPro	IPR002985	Arginine decarboxylase
194	216	PRINTS	PR01180	Arginine decarboxylase signature
194	216	InterPro	IPR002985	Arginine decarboxylase
321	338	PRINTS	PR01180	Arginine decarboxylase signature
321	338	InterPro	IPR002985	Arginine decarboxylase
170	191	PRINTS	PR01180	Arginine decarboxylase signature
170	191	InterPro	IPR002985	Arginine decarboxylase
462	483	PRINTS	PR01180	Arginine decarboxylase signature
462	483	InterPro	IPR002985	Arginine decarboxylase
144	159	PRINTS	PR01180	Arginine decarboxylase signature
144	159	InterPro	IPR002985	Arginine decarboxylase
540	561	PRINTS	PR01180	Arginine decarboxylase signature
540	561	InterPro	IPR002985	Arginine decarboxylase
66	81	PRINTS	PR01180	Arginine decarboxylase signature
66	81	InterPro	IPR002985	Arginine decarboxylase
66	343	SUPERFAMILY	SSF51419	PLP-binding barrel
66	343	InterPro	IPR029066	PLP-binding barrel
56	561	CDD	cd06830	PLPDE_III_ADC
56	561	InterPro	IPR002985	Arginine decarboxylase
446	566	FunFam	G3DSA:2.40.37.10:FF:000001	Biosynthetic arginine decarboxylase
360	455	FunFam	G3DSA:1.20.58.930:FF:000001	Biosynthetic arginine decarboxylase
98	116	PRINTS	PR01179	Ornithine/diaminopimelate/arginine (ODA) decarboxylase family signature
98	116	InterPro	IPR000183	Ornithine/DAP/Arg decarboxylase
331	350	PRINTS	PR01179	Ornithine/diaminopimelate/arginine (ODA) decarboxylase family signature
331	350	InterPro	IPR000183	Ornithine/DAP/Arg decarboxylase
120	132	PRINTS	PR01179	Ornithine/diaminopimelate/arginine (ODA) decarboxylase family signature
120	132	InterPro	IPR000183	Ornithine/DAP/Arg decarboxylase
540	553	PRINTS	PR01179	Ornithine/diaminopimelate/arginine (ODA) decarboxylase family signature
540	553	InterPro	IPR000183	Ornithine/DAP/Arg decarboxylase
237	250	PRINTS	PR01179	Ornithine/diaminopimelate/arginine (ODA) decarboxylase family signature
237	250	InterPro	IPR000183	Ornithine/DAP/Arg decarboxylase
67	343	FunFam	G3DSA:3.20.20.10:FF:000001	Biosynthetic arginine decarboxylase
67	343	Gene3D	G3DSA:3.20.20.10	Alanine racemase
67	343	InterPro	IPR029066	PLP-binding barrel
360	455	Gene3D	G3DSA:1.20.58.930	-
5	630	NCBIfam	TIGR01273	arginine decarboxylase
5	630	InterPro	IPR002985	Arginine decarboxylase
13	566	Gene3D	G3DSA:2.40.37.10	Lyase, Ornithine Decarboxylase; Chain A, domain 1
13	566	InterPro	IPR009006	Alanine racemase/group IV decarboxylase, C-terminal
1	632	PIRSF	PIRSF001336	ARGDC
1	632	InterPro	IPR002985	Arginine decarboxylase
580	629	Pfam	PF17944	Arginine decarboxylase C-terminal helical extension
580	629	InterPro	IPR041128	Arginine decarboxylase, C-terminal helical
2	631	Hamap	MF_01417	Biosynthetic arginine decarboxylase [speA].
2	631	InterPro	IPR002985	Arginine decarboxylase
275	288	ProSitePatterns	PS00879	Orn/DAP/Arg decarboxylases family 2 signature 2.
275	288	InterPro	IPR022657	Orn/DAP/Arg decarboxylase 2, conserved site
579	632	Gene3D	G3DSA:1.10.287.3440	-
366	452	Pfam	PF17810	Arginine decarboxylase helical bundle domain
366	452	InterPro	IPR040634	Arginine decarboxylase, helical bundle domain
98	116	ProSitePatterns	PS00878	Orn/DAP/Arg decarboxylases family 2 pyridoxal-P attachment site.
98	116	InterPro	IPR022653	Orn/DAP/Arg decarboxylase 2, pyridoxal-phosphate binding site

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

0.886

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Surrounding area

Pocket 2 P2Rank #2

0.547

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Surrounding area

Pocket 3 P2Rank #3

0.063

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Surrounding area

Pocket 4 P2Rank #4

0.052

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Surrounding area

Pocket 5 P2Rank #5

0.026

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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 #9

0.639

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Surrounding area

Residue sets

UniProt: Active site:502-502 Proton donor

UniProt: Binding site:281-291

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.859

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Surrounding area

Pocket 2 P2Rank #2

0.495

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Surrounding area

Pocket 3 P2Rank #3

0.069

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Surrounding area

Pocket 4 P2Rank #4

0.009

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Surrounding area

Pocket 5 P2Rank #5

0.008

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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_A0A0H3GT44	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_4106	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.

54 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 4 records from similar proteins

Structural ligands 4 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

AG2 PDB via homolog 130.2 Da · LogP -0.79 · TPSA 87.9 Open detail RCSB PDB

AZ1 PDB via homolog Detail RCSB PDB

LLP PDB via homolog Detail RCSB PDB

TME PDB via homolog Detail RCSB PDB

ZINC1529497 ZINC proposed compound · Tanimoto 1.000 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
AG2 RCSB PDB	3N2O	Q7MK24	130.2 Da LogP -0.79 TPSA 87.9	✓ Ro5	✓ Clean	`C(CCNC(=N)N)CN`
AZ1 RCSB PDB	1TUF	Q58497	188.2 Da LogP 1.89 TPSA 74.6	✓ Ro5	✓ Clean	`C(CCCC(=O)O)CCCC(=O)O`
LLP RCSB PDB	4XG1	A1SR00	375.3 Da LogP 0.71 TPSA 175.6	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)/C=N/CCCCC(C(=O)O)N)O`
TME RCSB PDB	4XG1	A1SR00	44.1 Da LogP 1.42 TPSA 0.0	✓ Ro5	✓ Clean	`CCC`

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
ZINC1529497 ZINC	1.000	230.3 Da LogP 3.06 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCC(=O)O`
ZINC1531045 ZINC	1.000	202.2 Da LogP 2.28 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCC(=O)O`
ZINC1593115 ZINC	1.000	216.3 Da LogP 2.67 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCC(=O)O`
ZINC1700020 ZINC	1.000	244.3 Da LogP 3.45 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCC(=O)O`
ZINC3860440 ZINC	1.000	258.4 Da LogP 3.84 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCC(=O)O`
ZINC3861298 ZINC	1.000	286.4 Da LogP 4.62 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCCC(=O)O`
ZINC5113062 ZINC	1.000	272.4 Da LogP 4.23 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCC(=O)O`
ZINC26897400 ZINC	0.800	286.4 Da LogP 3.41 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCCC(=O)CCCCCCC(=O)O`
ZINC3074813 ZINC	0.800	258.3 Da LogP 2.63 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCC(=O)CCCCCC(=O)O`
ZINC34423725 ZINC	0.800	342.5 Da LogP 4.97 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCC(=O)CCCCCCCCC(=O)O`
ZINC4822898 ZINC	0.800	272.3 Da LogP 3.02 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCCC(=O)CCCCCC(=O)O`
ZINC4822900 ZINC	0.800	300.4 Da LogP 3.80 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCC(=O)CCCCCC(=O)O`
ZINC13433578 ZINC	0.750	201.3 Da LogP 1.68 TPSA 80.4	✓ Ro5	✓ Clean	`NC(=O)CCCCCCCCC(=O)O`
ZINC14510370 ZINC	0.750	244.4 Da LogP 3.74 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCO`
ZINC1531061 ZINC	0.750	216.3 Da LogP 2.96 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCO`
ZINC1610426 ZINC	0.750	230.3 Da LogP 3.35 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCO`
ZINC2168567 ZINC	0.750	202.3 Da LogP 2.57 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCO`
ZINC3074815 ZINC	0.750	230.3 Da LogP 1.85 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCC(=O)CCCC(=O)O`
ZINC3861297 ZINC	0.750	272.4 Da LogP 4.52 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCCCO`
ZINC4284502 ZINC	0.750	258.4 Da LogP 4.13 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCCO`
ZINC5287109 ZINC	0.750	286.5 Da LogP 4.91 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCCCCO`
ZINC13545924 ZINC	0.737	214.3 Da LogP -0.10 TPSA 123.8	1 viol.	✓ Clean	`N=C(N)NCCCCCCCNC(=N)N`
ZINC1561855 ZINC	0.737	200.3 Da LogP -0.49 TPSA 123.8	1 viol.	✓ Clean	`N=C(N)NCCCCCCNC(=N)N`
ZINC2013578 ZINC	0.737	228.3 Da LogP 0.29 TPSA 123.8	1 viol.	✓ Clean	`N=C(N)NCCCCCCCCNC(=N)N`
ZINC3995661 ZINC	0.737	256.4 Da LogP 1.07 TPSA 123.8	1 viol.	✓ Clean	`N=C(N)NCCCCCCCCCCNC(=N)N`
ZINC2508031 ZINC	0.733	230.3 Da LogP 1.85 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCC(=O)CCCCC(=O)O`
ZINC2114966 ZINC	0.724	332.2 Da LogP 0.99 TPSA 149.5	✓ Ro5	✓ Clean	`Cc1ncc(COP(=O)(O)O)c(/C=N/CCCC(=O)O)c1O`
ZINC12954423 ZINC	0.706	232.4 Da LogP 3.90 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCS`
ZINC13357569 ZINC	0.706	243.4 Da LogP 3.71 TPSA 63.3	✓ Ro5	✓ Clean	`NCCCCCCCCCCCCCC(=O)O`
ZINC138216182 ZINC	0.706	293.2 Da LogP 4.76 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCBr`
ZINC14619253 ZINC	0.706	214.3 Da LogP 3.17 TPSA 54.4	✓ Ro5	✓ Clean	`CC(=O)CCCCCCCCCC(=O)O`
ZINC1529498 ZINC	0.706	200.3 Da LogP 3.99 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)O`
ZINC1530417 ZINC	0.706	228.4 Da LogP 4.77 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)O`
ZINC1628119 ZINC	0.706	214.3 Da LogP 4.38 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCC(=O)O`
ZINC1763117 ZINC	0.706	201.3 Da LogP 2.54 TPSA 63.3	✓ Ro5	✓ Clean	`NCCCCCCCCCCC(=O)O`
ZINC1841307 ZINC	0.706	228.3 Da LogP 3.56 TPSA 54.4	✓ Ro5	✓ Clean	`CC(=O)CCCCCCCCCCC(=O)O`
ZINC1845814 ZINC	0.706	215.3 Da LogP 2.93 TPSA 63.3	✓ Ro5	✓ Clean	`NCCCCCCCCCCCC(=O)O`
ZINC1845839 ZINC	0.706	200.3 Da LogP 2.78 TPSA 54.4	✓ Ro5	✓ Clean	`CC(=O)CCCCCCCCC(=O)O`
ZINC2164257 ZINC	0.706	218.4 Da LogP 3.51 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCS`
ZINC22048354 ZINC	0.706	229.4 Da LogP 3.32 TPSA 63.3	✓ Ro5	✓ Clean	`NCCCCCCCCCCCCC(=O)O`
ZINC33822328 ZINC	0.706	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CC(=O)CCCCCCCCCCCCCC(=O)O`
ZINC34552398 ZINC	0.706	257.4 Da LogP 4.10 TPSA 63.3	✓ Ro5	✓ Clean	`NCCCCCCCCCCCCCCC(=O)O`
ZINC34628306 ZINC	0.706	271.4 Da LogP 4.49 TPSA 63.3	✓ Ro5	✓ Clean	`NCCCCCCCCCCCCCCCC(=O)O`
ZINC35465466 ZINC	0.706	244.3 Da LogP 2.24 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCC(=O)CCC(=O)O`
ZINC5855130 ZINC	0.706	242.4 Da LogP 3.95 TPSA 54.4	✓ Ro5	✓ Clean	`CC(=O)CCCCCCCCCCCC(=O)O`
ZINC90745150 ZINC	0.706	260.4 Da LogP 4.68 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCS`
ZINC4789573 ZINC	0.667	310.4 Da LogP 4.62 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCC#CCCCCCCCC(=O)O`
ZINC5501162 ZINC	0.667	350.5 Da LogP 4.52 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCSCCCCCCSCCCCC(=O)O`
ZINC13742471 ZINC	0.636	299.5 Da LogP 0.66 TPSA 135.8	1 viol.	✓ Clean	`N=C(N)NCCCCCCNCCCCCCNC(=N)N`
ZINC5015111 ZINC	0.636	229.3 Da LogP -1.29 TPSA 135.8	1 viol.	✓ Clean	`N=C(N)NCCCCNCCCNC(=N)N`

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 A0A0H3GT44

Pathways

BioCyc ARGDECARBOX-RXN[CCO-PERI-BAC]-ARG/PROTON//AGMATHINE/CARBON-DIOXIDE.51. BioCyc ARGDECARBOX-RXN[CCO-CYTOSOL]-ARG/PROTON//AGMATHINE/CARBON-DIOXIDE.50.