KpATCC43816 Protein target profile

acetylglutamate kinase

Accession: VK055_3228

Gene: argB AIK81789.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism 1 reaction UniProt A0A0H3GPQ8

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Length 257

Pocket druggability (P2Rank · AlphaFold DB model) 0.888

Metabolic reactions 1

Chokepoint Yes

Direct ligand evidence 0 70 total records

Functional annotation 1 EC 5 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 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. 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: 2.7% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 33.992 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 95.12 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) 0.888

Structure A0A0H3GPQ8

Pocket Pocket 1

Druggability (FPocket) 0.386

Structure A0A0H3GPQ8

Pocket Pocket 2

ColabFold model

P2Rank 0.907 · Pocket 1

FPocket 0.288 · Pocket 3

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 129 / 4744 genomes with a hit

Prevalence 2.7%

Metabolic context

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

Explore metabolic network

Attractive metabolic target: catalyzes a producing & consuming chokepoint reaction in Arginine biosynthesis, no isoenzyme backup detected, 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.

MNPLIIKLGGVLLDSEEALERLFTALVNYREAHQRPLIIVHGGGCVVDELMKQLNLPVQKKNGLRVTPAEQIDIITGALAGTANKTLLAWAKKHGISSVGLFLGDGDSVKVTQLDAELGHVGLAQPGSPTLINTLLAGGYLPVVSSIGVTDEGQLMNVNADQAATALAATLGADLILLSDVSGILDGKGQRIAEMTAEKAEQLIEQGIITDGMIVKVNAALDAARALGRPVDIASWRHAEQLPALFNGTPIGTRILA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

2.7.2.8

Gene Ontology (GO)

GO:0003991 Catalysis of the reaction: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamate-5-phosphate.
GO:0006526 The chemical reactions and pathways resulting in the formation of arginine, 2-amino-5-(carbamimidamido)pentanoic acid.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0042450 OBSOLETE. The chemical reactions and pathways resulting in the formation of arginine (2-amino-5-guanidinopentanoic acid) via the intermediate compound ornithine.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

16 records

Show feature table

Start	End	DB	Term	Name
4	255	CDD	cd04249	AAK_NAGK-NC
4	255	InterPro	IPR041731	N-Acetyl-L-glutamate kinase, noncyclic
1	257	FunFam	G3DSA:3.40.1160.10:FF:000008	Acetylglutamate kinase
4	255	PANTHER	PTHR23342	N-ACETYLGLUTAMATE SYNTHASE
1	250	Hamap	MF_00082	Acetylglutamate kinase [argB].
1	250	InterPro	IPR037528	Acetylglutamate kinase ArgB
4	234	Pfam	PF00696	Amino acid kinase family
4	234	InterPro	IPR001048	Aspartate/glutamate/uridylate kinase
2	255	SUPERFAMILY	SSF53633	Carbamate kinase-like
2	255	InterPro	IPR036393	Acetylglutamate kinase-like superfamily
1	257	PIRSF	PIRSF000728	NAGK
1	257	InterPro	IPR004662	Acetylglutamate kinase family
1	257	Gene3D	G3DSA:3.40.1160.10	-
1	257	InterPro	IPR036393	Acetylglutamate kinase-like superfamily
4	233	NCBIfam	TIGR00761	acetylglutamate kinase
4	233	InterPro	IPR004662	Acetylglutamate kinase family

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.

Download VMD script Full viewer

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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

0.888

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Surrounding area

Pocket 2 P2Rank #2

0.033

Show in viewer

Surrounding area

Binding pockets · FPocket

Druggability (FPocket): high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Pocket 1 FPocket #2

0.386 Unusual size

Show in viewer

Surrounding area

Residue sets

UniProt: Binding site:157-157

UniProt: Binding site:180-185

UniProt: Binding site:208-210

UniProt: Binding site:43-44

UniProt: Binding site:65-65

UniProt: Site:216-216 Transition state stabilizer

UniProt: Site:7-7 Transition state stabilizer

Residue sets

UniProt: Binding site:157-157

UniProt: Binding site:180-185

UniProt: Binding site:208-210

UniProt: Binding site:43-44

UniProt: Binding site:65-65

UniProt: Site:216-216 Transition state stabilizer

UniProt: Site:7-7 Transition state stabilizer

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_A0A0H3GPQ8	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_3228	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.

70 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 20 records from similar proteins

Structural ligands 20 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

14N PDB via homolog 220.3 Da · LogP 1.14 · TPSA 43.8 Open detail RCSB PDB

5RN PDB via homolog Detail RCSB PDB

97Q PDB via homolog Detail RCSB PDB

97T PDB via homolog Detail RCSB PDB

97W 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
14N RCSB PDB	7NLT	P9WQ01	220.3 Da LogP 1.14 TPSA 43.8	✓ Ro5	✓ Clean	`CN1CCN(CC1)c2ccc(cc2)C(=O)O`
5RN RCSB PDB	7NLU	P9WQ01	159.2 Da LogP 2.37 TPSA 32.9	✓ Ro5	✓ Clean	`CC(=O)c1c[nH]c2c1cccc2`
97Q RCSB PDB	7NNB	P9WQ01	281.2 Da LogP 3.98 TPSA 33.1	✓ Ro5	✓ Clean	`c1cc2c(cc(nc2c(c1)C(F)(F)F)C(F)(F)F)O`
97T RCSB PDB	7NLQ	P9WQ01	161.2 Da LogP 2.05 TPSA 46.3	✓ Ro5	✓ Clean	`c1ccc(c(c1)c2ccno2)O`
97W RCSB PDB	7NLX	P9WQ01	213.2 Da LogP 2.96 TPSA 33.1	✓ Ro5	✓ Clean	`c1cc2c(ccnc2cc1C(F)(F)F)O`
98K RCSB PDB	7NLY	P9WQ01	152.6 Da LogP 2.22 TPSA 28.7	✓ Ro5	✓ Clean	`c1ccc2c(c1)[nH]c(n2)Cl`
98Q RCSB PDB	7NLZ	P9WQ01	215.2 Da LogP 3.20 TPSA 25.0	✓ Ro5	✓ Clean	`COc1cc2cc[nH]c2cc1C(F)(F)F`
98T RCSB PDB	7NLS	P9WQ01	278.0 Da LogP 1.78 TPSA 46.5	✓ Ro5	✓ Clean	`COC(=O)c1ccc(c(c1)I)O`
98W RCSB PDB	7NN7	P9WQ01	210.2 Da LogP 0.97 TPSA 72.8	✓ Ro5	✓ Clean	`COC(=O)c1cc(cc(c1)O)C(=O)OC`
98Z RCSB PDB	7NN8	P9WQ01	142.2 Da LogP 2.04 TPSA 39.6	✓ Ro5	✓ Clean	`c1ccc2c(c1)c(c[nH]2)C#N`
9EQ RCSB PDB	7NM0	P9WQ01	152.1 Da LogP 1.30 TPSA 57.5	✓ Ro5	✓ Clean	`CC(=O)c1c(cccc1O)O`
ANP RCSB PDB	1GS5	P0A6C8	506.2 Da LogP -2.06 TPSA 281.9	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
DTU RCSB PDB	2WXB	P0A6C8	154.3 Da LogP -0.43 TPSA 40.5	✓ Ro5	✓ Clean	`C([C@H]([C@H](CS)O)O)S`
GGB RCSB PDB	7NLP	P9WQ01	176.2 Da LogP -1.80 TPSA 134.5	✓ Ro5	✓ Clean	`[H]/N=C(\N)/NOCC[C@@H](C(=O)O)N`
NHE RCSB PDB	7NLO	P9WQ01	207.3 Da LogP 0.80 TPSA 66.4	✓ Ro5	✓ Clean	`C1CCC(CC1)NCCS(=O)(=O)O`
NLG RCSB PDB	1GS5	P0A6C8	189.2 Da LogP -0.56 TPSA 103.7	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](CCC(=O)O)C(=O)O`
PIY RCSB PDB	7NLR	P9WQ01	144.2 Da LogP 2.08 TPSA 28.7	✓ Ro5	✓ Clean	`c1ccc(cc1)c2[nH]ccn2`
SRT RCSB PDB	3T7B	Q8ZA87	150.1 Da LogP -2.12 TPSA 115.1	✓ Ro5	✓ Clean	`[C@H]([C@H](C(=O)O)O)(C(=O)O)O`
UOK RCSB PDB	7NLW	P9WQ01	186.2 Da LogP 2.24 TPSA 48.8	✓ Ro5	✓ Clean	`COc1ccc2c(c1)c(c[nH]2)CC#N`
X2W RCSB PDB	2X2W	P0A6C8	269.1 Da LogP -1.01 TPSA 150.2	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](CCC(=O)OP(=O)(O)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).

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
ZINC158905 ZINC	1.000	220.3 Da LogP 1.14 TPSA 43.8	✓ Ro5	✓ Clean	`CN1CCN(c2ccc(C(=O)O)cc2)CC1`
ZINC1710230 ZINC	1.000	207.3 Da LogP 0.80 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCNC1CCCCC1`
ZINC2548331 ZINC	1.000	278.0 Da LogP 1.78 TPSA 46.5	✓ Ro5	✓ Clean	`COC(=O)c1ccc(O)c(I)c1`
ZINC32327 ZINC	1.000	210.2 Da LogP 0.97 TPSA 72.8	✓ Ro5	✓ Clean	`COC(=O)c1cc(O)cc(C(=O)OC)c1`
ZINC34503706 ZINC	1.000	215.2 Da LogP 3.20 TPSA 25.0	✓ Ro5	✓ Clean	`COc1cc2cc[nH]c2cc1C(F)(F)F`
ZINC8830538 ZINC	1.000	281.2 Da LogP 3.98 TPSA 33.1	✓ Ro5	✓ Clean	`Oc1cc(C(F)(F)F)nc2c(C(F)(F)F)cccc12`
ZINC89202735 ZINC	0.913	220.3 Da LogP 3.74 TPSA 28.7	✓ Ro5	✓ Clean	`c1ccc(-c2ccc(-c3ncc[nH]3)cc2)cc1`
ZINC12370640 ZINC	0.862	234.3 Da LogP 1.53 TPSA 43.8	✓ Ro5	✓ Clean	`CN1CCCN(c2ccc(C(=O)O)cc2)CC1`
ZINC1532510 ZINC	0.821	304.3 Da LogP -1.60 TPSA 170.1	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CCC(=O)O)C(=…`
ZINC1532511 ZINC	0.821	304.3 Da LogP -1.60 TPSA 170.1	✓ Ro5	✓ Clean	`CC(=O)N[C@H](CC(=O)O)C(=O)N[C@@H](CCC(=O)O)C(=O…`
ZINC1532512 ZINC	0.821	304.3 Da LogP -1.60 TPSA 170.1	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](CC(=O)O)C(=O)N[C@H](CCC(=O)O)C(=O…`
ZINC1532513 ZINC	0.821	304.3 Da LogP -1.60 TPSA 170.1	✓ Ro5	✓ Clean	`CC(=O)N[C@H](CC(=O)O)C(=O)N[C@H](CCC(=O)O)C(=O)O`
ZINC12360002 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12360703 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12503599 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC16546165 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@](=O)(O)OP(=O)(…`
ZINC31977053 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC4806433 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC53683898 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586019 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC8586020 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586021 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)OP(=O…`
ZINC8586022 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC56412 ZINC	0.800	252.2 Da LogP 1.05 TPSA 78.9	✓ Ro5	✓ Clean	`COC(=O)c1cc(C(=O)OC)cc(C(=O)OC)c1`
ZINC2504638 ZINC	0.793	304.3 Da LogP -1.60 TPSA 170.1	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](CC(=O)N[C@@H](CCC(=O)O)C(=O)O)C(=…`
ZINC4534089 ZINC	0.793	304.3 Da LogP -1.60 TPSA 170.1	✓ Ro5	✓ Clean	`CC(=O)N[C@H](CC(=O)N[C@@H](CCC(=O)O)C(=O)O)C(=O…`
ZINC4534090 ZINC	0.793	304.3 Da LogP -1.60 TPSA 170.1	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](CC(=O)N[C@H](CCC(=O)O)C(=O)O)C(=O…`
ZINC4534091 ZINC	0.793	304.3 Da LogP -1.60 TPSA 170.1	✓ Ro5	✓ Clean	`CC(=O)N[C@H](CC(=O)N[C@H](CCC(=O)O)C(=O)O)C(=O)O`
ZINC2004372 ZINC	0.786	221.3 Da LogP 1.19 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCCNC1CCCCC1`
ZINC38364153 ZINC	0.786	235.3 Da LogP 1.58 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCCCNC1CCCCC1`
ZINC169847 ZINC	0.759	218.3 Da LogP 1.64 TPSA 23.6	✓ Ro5	✓ Clean	`CC(=O)c1ccc(N2CCN(C)CC2)cc1`
ZINC15923743 ZINC	0.743	227.2 Da LogP 3.27 TPSA 33.1	✓ Ro5	✓ Clean	`Cc1cccc2c(O)cc(C(F)(F)F)nc12`
ZINC13518964 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC1532515 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@H](O…`
ZINC1571045 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC1842158 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@H](O…`
ZINC2046931 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC2126310 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3201891 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC3201893 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3830180 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3860156 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3977897 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](COP(=O)(O)O)[C@@H](O…`
ZINC4806442 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC8613167 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC2560824 ZINC	0.733	260.2 Da LogP -1.05 TPSA 132.8	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](C)C(=O)N[C@@H](CCC(=O)O)C(=O)O`
ZINC82264502 ZINC	0.733	219.3 Da LogP 0.54 TPSA 49.6	✓ Ro5	✓ Clean	`CN1CCN(c2ccc(C(N)=O)cc2)CC1`
ZINC8700304 ZINC	0.733	278.0 Da LogP 1.78 TPSA 46.5	✓ Ro5	✓ Clean	`COC(=O)c1ccc(I)c(O)c1`
ZINC58123315 ZINC	0.731	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(=…`
ZINC58123326 ZINC	0.731	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(=…`

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 A0A0H3GPQ8

Pathways

KEGG R02649 BioCyc ACETYLGLUTKIN-RXN