KpATCC43816 Protein target profile

succinylarginine dihydrolase

Accession: VK055_1234

Gene: astB2 AIK79857.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism 1 reaction UniProt A0A0H3GVX4

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Length 441

Pocket druggability (P2Rank · AlphaFold DB model) 0.665

Metabolic reactions 1

Chokepoint Yes

Direct ligand evidence 0 52 total records

Functional annotation 1 EC 4 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 89.7% 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: 2.3% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 76.19 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 97.8 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) 0.665

Structure A0A0H3GVX4

Pocket Pocket 1

Druggability (FPocket) 0.318

Structure A0A0H3GVX4

Pocket Pocket 7

ColabFold model

P2Rank 0.613 · Pocket 1

FPocket 0.148 · Pocket 7

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 111 / 4744 genomes with a hit

Prevalence 2.3%

Metabolic context

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

Explore metabolic network

Attractive metabolic target: catalyzes a consuming chokepoint reaction in Arginine and proline metabolism, more central than 89.7% of genes in this genome, no human homolog detected.

Relative network centrality 89.7% more central than 89.7% of genes in this genome

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MTAREVNFDGLPGLTHHYAGLSFGNEASTRHRYRVSNPQLAAKQGLKKMKALADAGYPQAVIPPQERPNVPLLRQLGFSGSDEQVVARVAQQEPDLLSAVSSASAMWVANAATVCPSADSLDGLVHLTVANLQDKFHRASEAPTTEALLQAIFPDRTRFAIHPALPASAWFGDEGAANHNRLGGEYGAPGVQLFVYGRRRGSEEAPRRYPARQTLEASQAVARLNQVNPRQLIFARQHPAAIDTGVFHNDVIAVSNRQVLFCHEQAFADQTALLQQLAQRVPGFTPLVVPASRVSVAEAVATYLFNSQLLSRADGSMALILPQEAQEHAGVWEYLNELLAGDNPIADLRVFDLRESMANGGGPACLRLRVVLTAEEYQAVNPHVLMNDTLFATLNDWVDRYYRDRLTQADLADPQLLREGRDALDRLTQILQLGSVYPFQQ

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 4 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

3.5.3.23

Gene Ontology (GO)

GO:0006525 The chemical reactions and pathways involving arginine, 2-amino-5-(carbamimidamido)pentanoic acid.
GO:0009015 Catalysis of the reaction: N(2)-succinyl-L-arginine + 2 H2O + 2 H+ = N(2)-succinyl-L-ornithine + CO2 + 2 NH4.
GO:0019544 OBSOLETE. The chemical reactions and pathways resulting in the breakdown of L-arginine into other compounds, including L-glutamate.
GO:0019545 OBSOLETE. The chemical reactions and pathways resulting in the breakdown of L-arginine into other compounds, including succinate.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

10 records

Show feature table

Start	End	DB	Term	Name
1	441	PANTHER	PTHR30420	N-SUCCINYLARGININE DIHYDROLASE
4	440	NCBIfam	TIGR03241	N-succinylarginine dihydrolase
4	440	InterPro	IPR007079	Succinylarginine dihydrolase
1	441	Hamap	MF_01172	N-succinylarginine dihydrolase [astB].
1	441	InterPro	IPR007079	Succinylarginine dihydrolase
1	441	Gene3D	G3DSA:3.75.10.20	Succinylarginine dihydrolase
1	441	InterPro	IPR037031	Succinylarginine dihydrolase superfamily
3	441	SUPERFAMILY	SSF55909	Pentein
3	440	Pfam	PF04996	Succinylarginine dihydrolase
3	440	InterPro	IPR007079	Succinylarginine dihydrolase

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

0.665

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Surrounding area

Pocket 2 P2Rank #2

0.051

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Surrounding area

Pocket 3 P2Rank #3

0.033

Likely same site as FPocket 1 2.1 Å 8 shared residues 100% of smaller site

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Surrounding area

Pocket 4 P2Rank #4

0.002

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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 #7

0.318

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Surrounding area

Pocket 2 FPocket #1

0.243

Likely same site as P2Rank 3 2.1 Å 8 shared residues 100% of smaller site

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Surrounding area

Residue sets

UniProt: Active site:174-174

UniProt: Active site:248-248

UniProt: Active site:365-365 Nucleophile

UniProt: Binding site:110-110

UniProt: Binding site:137-138

UniProt: Binding site:19-28

UniProt: Binding site:212-212

UniProt: Binding site:250-250

UniProt: Binding site:359-359

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.613

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Surrounding area

Pocket 2 P2Rank #2

0.07

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Surrounding area

Pocket 3 P2Rank #3

0.059

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Surrounding area

Residue sets

UniProt: Active site:174-174

UniProt: Active site:248-248

UniProt: Active site:365-365 Nucleophile

UniProt: Binding site:110-110

UniProt: Binding site:137-138

UniProt: Binding site:19-28

UniProt: Binding site:212-212

UniProt: Binding site:250-250

UniProt: Binding site:359-359

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_A0A0H3GVX4	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_1234	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

SUG PDB via homolog 274.3 Da · LogP -1.32 · TPSA 165.6 Open detail RCSB PDB

SUO PDB via homolog Detail RCSB PDB

ZINC1529628 ZINC proposed compound · Tanimoto 1.000 Detail ZINC

ZINC2383349774 ZINC proposed compound · Tanimoto 0.838 Detail ZINC

ZINC1866114950 ZINC proposed compound · Tanimoto 0.758 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
SUG RCSB PDB	1YNI	P76216	274.3 Da LogP -1.32 TPSA 165.6	1 viol.	✓ Clean	`C(C[C@@H](C(=O)O)NC(=O)CCC(=O)O)CNC(=N)N`
SUO RCSB PDB	1YNH	P76216	232.2 Da LogP -0.84 TPSA 129.7	✓ Ro5	✓ Clean	`C(C[C@@H](C(=O)O)NC(=O)CCC(=O)O)CN`

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
ZINC1529628 ZINC	1.000	274.3 Da LogP -1.32 TPSA 165.6	1 viol.	✓ Clean	`N=C(N)NCCC[C@H](NC(=O)CCC(=O)O)C(=O)O`
ZINC2383349774 ZINC	0.838	330.4 Da LogP 0.24 TPSA 165.6	1 viol.	✓ Clean	`N=C(N)NCCC[C@H](NC(=O)CCCCCCC(=O)O)C(=O)O`
ZINC1866114950 ZINC	0.758	260.3 Da LogP -0.06 TPSA 129.7	✓ Ro5	✓ Clean	`NCCCC[C@H](NC(=O)CCCC(=O)O)C(=O)O`
ZINC15261332 ZINC	0.744	303.3 Da LogP -1.99 TPSA 191.6	1 viol.	✓ Clean	`N=C(N)NCCC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)O`
ZINC1576211 ZINC	0.730	231.3 Da LogP -2.22 TPSA 154.3	1 viol.	✓ Clean	`N=C(N)NCCC[C@H](NC(=O)CN)C(=O)O`
ZINC1530138 ZINC	0.719	217.3 Da LogP -0.97 TPSA 118.4	✓ Ro5	✓ Clean	`NCCCC[C@H](NC(=O)CCN)C(=O)O`
ZINC100008960 ZINC	0.707	356.5 Da LogP 2.74 TPSA 128.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)N[C@H](CCCNC(=N)N)C(=O)O`
ZINC70669861 ZINC	0.707	356.5 Da LogP 2.74 TPSA 128.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)N[C@@H](CCCNC(=N)N)C(=O)O`
ZINC85738396 ZINC	0.707	384.6 Da LogP 3.52 TPSA 128.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)N[C@@H](CCCNC(=N)N)C(=O)O`
ZINC15261541 ZINC	0.706	261.3 Da LogP -1.51 TPSA 155.7	✓ Ro5	✓ Clean	`NCCC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)O`
ZINC1847640 ZINC	0.703	216.2 Da LogP -1.16 TPSA 128.3	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](CCCNC(=N)N)C(=O)O`
ZINC2169795 ZINC	0.703	216.2 Da LogP -1.16 TPSA 128.3	✓ Ro5	✓ Clean	`CC(=O)N[C@H](CCCNC(=N)N)C(=O)O`
ZINC1530296 ZINC	0.700	247.2 Da LogP -0.71 TPSA 141.0	✓ Ro5	✓ Clean	`O=C(O)CCC(=O)N[C@@H](CCC(=O)O)C(=O)O`
ZINC6783254 ZINC	0.697	231.2 Da LogP 0.61 TPSA 103.7	✓ Ro5	✓ Clean	`CCCC[C@H](NC(=O)CCC(=O)O)C(=O)O`
ZINC6783285 ZINC	0.697	231.2 Da LogP 0.61 TPSA 103.7	✓ Ro5	✓ Clean	`CCCC[C@@H](NC(=O)CCC(=O)O)C(=O)O`
ZINC1722125 ZINC	0.694	217.2 Da LogP -1.63 TPSA 154.3	1 viol.	✓ Clean	`N=C(N)NCCC[C@H](NC(N)=O)C(=O)O`
ZINC4537126 ZINC	0.694	217.2 Da LogP -1.63 TPSA 154.3	1 viol.	✓ Clean	`N=C(N)NCCC[C@@H](NC(N)=O)C(=O)O`
ZINC1529261 ZINC	0.684	304.3 Da LogP -1.39 TPSA 185.8	1 viol.	✓ Clean	`N=C(N)NCCC[C@@H](N[C@@H](CCC(=O)O)C(=O)O)C(=O)O`
ZINC1529262 ZINC	0.684	304.3 Da LogP -1.39 TPSA 185.8	1 viol.	✓ Clean	`N=C(N)NCCC[C@@H](N[C@H](CCC(=O)O)C(=O)O)C(=O)O`
ZINC1529939 ZINC	0.684	304.3 Da LogP -1.39 TPSA 185.8	1 viol.	✓ Clean	`N=C(N)NCCC[C@H](N[C@@H](CCC(=O)O)C(=O)O)C(=O)O`
ZINC1529940 ZINC	0.684	304.3 Da LogP -1.39 TPSA 185.8	1 viol.	✓ Clean	`N=C(N)NCCC[C@H](N[C@H](CCC(=O)O)C(=O)O)C(=O)O`
ZINC1530510 ZINC	0.684	246.3 Da LogP -1.23 TPSA 148.5	1 viol.	✓ Clean	`N=C(N)NCCC[C@H](NCCC(=O)O)C(=O)O`
ZINC141957116 ZINC	0.667	342.5 Da LogP 4.00 TPSA 92.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)N[C@@H](CCCN)C(=O)O`
ZINC58123315 ZINC	0.667	376.3 Da LogP -1.36 TPSA 207.4	1 viol.	✓ Clean	`O=C(O)CC[C@H](NC(=O)CCC(=O)N[C@@H](CCC(=O)O)C(=…`
ZINC58123320 ZINC	0.667	376.3 Da LogP -1.36 TPSA 207.4	1 viol.	✓ Clean	`O=C(O)CC[C@H](NC(=O)CCC(=O)N[C@H](CCC(=O)O)C(=O…`
ZINC58123326 ZINC	0.667	376.3 Da LogP -1.36 TPSA 207.4	1 viol.	✓ Clean	`O=C(O)CC[C@@H](NC(=O)CCC(=O)N[C@H](CCC(=O)O)C(=…`
ZINC78044048 ZINC	0.667	342.5 Da LogP 4.00 TPSA 92.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)N[C@H](CCCN)C(=O)O`
ZINC1576188 ZINC	0.659	288.3 Da LogP -3.11 TPSA 183.4	1 viol.	✓ Clean	`N=C(N)NCCC[C@H](NC(=O)CNC(=O)CN)C(=O)O`
ZINC5502067 ZINC	0.659	288.3 Da LogP -3.11 TPSA 183.4	1 viol.	✓ Clean	`N=C(N)NCCC[C@@H](NC(=O)CNC(=O)CN)C(=O)O`
ZINC39798595 ZINC	0.644	360.4 Da LogP -2.87 TPSA 220.7	1 viol.	✓ Clean	`N=C(N)NCCC[C@H](N)C(=O)NCC(=O)N[C@@H](CCC(=O)O)…`
ZINC1731788 ZINC	0.643	303.3 Da LogP -1.99 TPSA 191.6	1 viol.	✓ Clean	`N=C(N)NCCC[C@H](N)C(=O)N[C@@H](CCC(=O)O)C(=O)O`
ZINC1731789 ZINC	0.643	303.3 Da LogP -1.99 TPSA 191.6	1 viol.	✓ Clean	`N=C(N)NCCC[C@@H](N)C(=O)N[C@@H](CCC(=O)O)C(=O)O`
ZINC5113904 ZINC	0.639	261.3 Da LogP -1.51 TPSA 155.7	✓ Ro5	✓ Clean	`NCCC[C@H](NC(=O)[C@@H](N)CCC(=O)O)C(=O)O`
ZINC147300883 ZINC	0.636	217.2 Da LogP 0.22 TPSA 103.7	✓ Ro5	✓ Clean	`CCC[C@@H](NC(=O)CCC(=O)O)C(=O)O`
ZINC24803120 ZINC	0.636	217.2 Da LogP 0.22 TPSA 103.7	✓ Ro5	✓ Clean	`CCC[C@H](NC(=O)CCC(=O)O)C(=O)O`
ZINC116981435 ZINC	0.629	319.3 Da LogP -0.81 TPSA 179.0	1 viol.	✓ Clean	`NCCCC[C@@H](NC(=O)N[C@@H](CCC(=O)O)C(=O)O)C(=O)O`
ZINC116981437 ZINC	0.629	319.3 Da LogP -0.81 TPSA 179.0	1 viol.	✓ Clean	`NCCCC[C@@H](NC(=O)N[C@H](CCC(=O)O)C(=O)O)C(=O)O`
ZINC116981440 ZINC	0.629	319.3 Da LogP -0.81 TPSA 179.0	1 viol.	✓ Clean	`NCCCC[C@H](NC(=O)N[C@H](CCC(=O)O)C(=O)O)C(=O)O`
ZINC40860752 ZINC	0.629	319.3 Da LogP -0.81 TPSA 179.0	1 viol.	✓ Clean	`NCCCC[C@H](NC(=O)N[C@@H](CCC(=O)O)C(=O)O)C(=O)O`
ZINC225926188 ZINC	0.625	404.4 Da LogP -0.58 TPSA 207.4	1 viol.	✓ Clean	`O=C(O)CC[C@H](NC(=O)CCCCC(=O)N[C@@H](CCC(=O)O)C…`
ZINC225926203 ZINC	0.625	404.4 Da LogP -0.58 TPSA 207.4	1 viol.	✓ Clean	`O=C(O)CC[C@H](NC(=O)CCCCC(=O)N[C@H](CCC(=O)O)C(…`
ZINC225926220 ZINC	0.625	404.4 Da LogP -0.58 TPSA 207.4	1 viol.	✓ Clean	`O=C(O)CC[C@@H](NC(=O)CCCCC(=O)N[C@H](CCC(=O)O)C…`
ZINC225956936 ZINC	0.625	390.3 Da LogP -0.97 TPSA 207.4	1 viol.	✓ Clean	`O=C(O)CC[C@H](NC(=O)CCCC(=O)N[C@@H](CCC(=O)O)C(…`
ZINC225956945 ZINC	0.625	390.3 Da LogP -0.97 TPSA 207.4	1 viol.	✓ Clean	`O=C(O)CC[C@H](NC(=O)CCCC(=O)N[C@H](CCC(=O)O)C(=…`
ZINC225956959 ZINC	0.625	390.3 Da LogP -0.97 TPSA 207.4	1 viol.	✓ Clean	`O=C(O)CC[C@@H](NC(=O)CCCC(=O)N[C@H](CCC(=O)O)C(…`
ZINC5706877 ZINC	0.625	330.4 Da LogP -2.59 TPSA 216.2	1 viol.	✓ Clean	`N=C(N)NCCC[C@H](N)C(=O)N[C@@H](CCCNC(=N)N)C(=O)O`
ZINC13514809 ZINC	0.622	404.4 Da LogP -1.77 TPSA 222.1	1 viol.	✓ Clean	`NCCCC[C@H](NC(=O)CC[C@H](NC(=O)CC[C@H](N)C(=O)O…`
ZINC2579085 ZINC	0.610	245.3 Da LogP -1.83 TPSA 154.3	1 viol.	✓ Clean	`C[C@H](N)C(=O)N[C@@H](CCCNC(=N)N)C(=O)O`
ZINC8577164 ZINC	0.610	245.3 Da LogP -1.83 TPSA 154.3	1 viol.	✓ Clean	`C[C@@H](N)C(=O)N[C@@H](CCCNC(=N)N)C(=O)O`
ZINC1857792174 ZINC	0.609	374.4 Da LogP -0.99 TPSA 187.9	1 viol.	✓ Clean	`CC(C)[C@@H](NC(=O)CCC(=O)O)C(=O)N[C@@H](CCCNC(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 A0A0H3GVX4

Pathways

KEGG R04189 BioCyc SUCCARGDIHYDRO-RXN