KpATCC43816 Protein target profile

N-acetyl-gamma-glutamyl-phosphate reductase

Accession: VK055_3229

Gene: argC AIK81790.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism 1 reaction UniProt A0A0H3GH05

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Length 334

Pocket druggability (P2Rank · AlphaFold DB model) 0.937

Metabolic reactions 1

Chokepoint Yes

Direct ligand evidence 0 58 total records

Functional annotation 1 EC 8 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 91.1% 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: 3.1% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 87.725 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 98.43 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) 0.937

Structure A0A0H3GH05

Pocket Pocket 1

Druggability (FPocket) 0.239

Structure A0A0H3GH05

Pocket Pocket 11

ColabFold model

P2Rank 0.919 · Pocket 1

FPocket 0.416 · Pocket 16

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 147 / 4744 genomes with a hit

Prevalence 3.1%

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 biosynthesis, no isoenzyme backup detected, more central than 91.1% of genes in this genome, no human homolog detected.

Relative network centrality 91.1% more central than 91.1% of genes in this genome

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MLNTLIVGASGYAGAELVTYINRHPHMNITALTVSAQSNDAGKLISDLHPQLKGIVDMPLQPMSDISEFSAGVDVVFLATAHEVSHDLAPQFLAAGCVVFDLSGAFRVNDGAFYEKYYGFTHRHPDLLKQAVYGLAEWSADALKDAQLIAVPGCYPTAAQLSLKPLIEANLLDLNQWPVINATSGVSGAGRKAAIGNSFCEVSLQPYGIFNHRHQPEIASHLGAKVIFTPHLGNFKRGILETITCRLKPGVGHAQIAAVYQQAYADKPLVRLYDKGVPALKSVEGLPFCDIGFAVQDDHLIVVTAEDNLLKGAAAQAVQCANIRFGFAETQSLI

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

1.2.1.38

Gene Ontology (GO)

GO:0016620 Catalysis of an oxidation-reduction (redox) reaction in which an aldehyde or ketone (oxo) group acts as a hydrogen or electron donor and reduces NAD or NADP.
GO:0051287 Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH.
GO:0006526 The chemical reactions and pathways resulting in the formation of arginine, 2-amino-5-(carbamimidamido)pentanoic acid.
GO:0046983 The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits.
GO:0008652 The chemical reactions and pathways resulting in the formation of amino acids, organic acids containing one or more amino substituents.
GO:0070401 Binding to the oxidized form, NADP+, of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions.
GO:0003942 Catalysis of the reaction: N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate = N-acetyl-5-glutamyl phosphate + NADPH + H+.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

20 records

Show feature table

Start	End	DB	Term	Name
153	312	Gene3D	G3DSA:3.30.360.10	Dihydrodipicolinate Reductase; domain 2
3	333	NCBIfam	TIGR01850	N-acetyl-gamma-glutamyl-phosphate reductase
3	333	InterPro	IPR000706	N-acetyl-gamma-glutamyl-phosphate reductase, type 1
1	171	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
1	171	InterPro	IPR036291	NAD(P)-binding domain superfamily
6	330	Gene3D	G3DSA:3.40.50.720	-
2	334	Hamap	MF_00150	N-acetyl-gamma-glutamyl-phosphate reductase [argC].
2	334	InterPro	IPR000706	N-acetyl-gamma-glutamyl-phosphate reductase, type 1
163	311	Pfam	PF02774	Semialdehyde dehydrogenase, dimerisation domain
163	311	InterPro	IPR012280	Semialdehyde dehydrogenase, dimerisation domain
149	165	ProSitePatterns	PS01224	N-acetyl-gamma-glutamyl-phosphate reductase active site.
149	165	InterPro	IPR023013	N-acetyl-gamma-glutamyl-phosphate reductase, active site
154	308	SUPERFAMILY	SSF55347	Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain
3	333	PANTHER	PTHR32338	N-ACETYL-GAMMA-GLUTAMYL-PHOSPHATE REDUCTASE, CHLOROPLASTIC-RELATED-RELATED
152	308	FunFam	G3DSA:3.30.360.10:FF:000014	N-acetyl-gamma-glutamyl-phosphate reductase
3	146	SMART	SM00859	Semialdhyde_dh_3
3	146	InterPro	IPR000534	Semialdehyde dehydrogenase, NAD-binding
5	146	Pfam	PF01118	Semialdehyde dehydrogenase, NAD binding domain
5	146	InterPro	IPR000534	Semialdehyde dehydrogenase, NAD-binding
4	164	FunFam	G3DSA:3.40.50.720:FF:000117	N-acetyl-gamma-glutamyl-phosphate reductase

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

0.937

Show in viewer

Surrounding area

Pocket 2 P2Rank #2

0.009

Show in viewer

Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #11

0.239

Show in viewer

Surrounding area

Residue sets

UniProt: Active site:154-154

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_A0A0H3GH05	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_3229	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

AZI PDB via homolog 42.0 Da · LogP 0.87 · TPSA 58.7 Open detail RCSB PDB

BTB PDB via homolog Detail RCSB PDB

MLA PDB via homolog Detail RCSB PDB

MLT PDB via homolog Detail RCSB PDB

MYI 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
AZI RCSB PDB	2OZP	Q5SH26	42.0 Da LogP 0.87 TPSA 58.7	✓ Ro5	Alert	`[N-]=[N+]=[N-]`
BTB RCSB PDB	2I3A	P9WPZ9	209.2 Da LogP -3.01 TPSA 104.4	✓ Ro5	✓ Clean	`C(CO)N(CCO)C(CO)(CO)CO`
MLA RCSB PDB	1YS4	Q57658	104.1 Da LogP -0.45 TPSA 74.6	✓ Ro5	✓ Clean	`C(C(=O)O)C(=O)O`
MLT RCSB PDB	3DR3	P59310	134.1 Da LogP -1.09 TPSA 94.8	✓ Ro5	✓ Clean	`C([C@H](C(=O)O)O)C(=O)O`
MYI RCSB PDB	7NOT	P9WPZ9	205.2 Da LogP 1.80 TPSA 62.3	✓ Ro5	✓ Clean	`COc1ccc2c(c1)c(c[nH]2)CC(=O)O`
UJQ RCSB PDB	7NNR	P9WPZ9	226.2 Da LogP 3.01 TPSA 46.5	✓ Ro5	✓ Clean	`c1ccc2c(c1)C(c3ccccc3O2)C(=O)O`
UKE RCSB PDB	7NPH	P9WPZ9	193.2 Da LogP 1.53 TPSA 72.6	✓ Ro5	✓ Clean	`COc1ccc2c(c1)nc(o2)C(=O)O`
UKK RCSB PDB	7NPJ	P9WPZ9	186.2 Da LogP 2.46 TPSA 48.1	✓ Ro5	Alert	`c1ccc(cc1)Oc2ccc(cn2)N`

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
ZINC1615342 ZINC	1.000	209.2 Da LogP -3.01 TPSA 104.4	✓ Ro5	✓ Clean	`OCCN(CCO)C(CO)(CO)CO`
ZINC57162 ZINC	1.000	205.2 Da LogP 1.80 TPSA 62.3	✓ Ro5	✓ Clean	`COc1ccc2[nH]cc(CC(=O)O)c2c1`
ZINC78659 ZINC	1.000	226.2 Da LogP 3.01 TPSA 46.5	✓ Ro5	✓ Clean	`O=C(O)C1c2ccccc2Oc2ccccc21`
ZINC20278485 ZINC	0.800	262.3 Da LogP 4.12 TPSA 48.1	✓ Ro5	Alert	`Nc1ccc(Oc2ccc(-c3ccccc3)cc2)nc1`
ZINC195148 ZINC	0.789	219.2 Da LogP 2.19 TPSA 62.3	✓ Ro5	✓ Clean	`COc1ccc2[nH]cc(CCC(=O)O)c2c1`
ZINC14455597 ZINC	0.784	219.2 Da LogP 1.89 TPSA 51.3	✓ Ro5	✓ Clean	`COC(=O)Cc1c[nH]c2ccc(OC)cc12`
ZINC394015 ZINC	0.784	204.2 Da LogP 1.20 TPSA 68.1	✓ Ro5	✓ Clean	`COc1ccc2[nH]cc(CC(N)=O)c2c1`
ZINC9970383 ZINC	0.778	205.2 Da LogP 1.80 TPSA 62.3	✓ Ro5	✓ Clean	`COc1ccc2c(CC(=O)O)c[nH]c2c1`
ZINC66354646 ZINC	0.757	207.2 Da LogP 1.62 TPSA 61.6	✓ Ro5	✓ Clean	`COC(=O)c1nc2cc(OC)ccc2o1`
ZINC2512932 ZINC	0.750	233.3 Da LogP 2.58 TPSA 62.3	✓ Ro5	✓ Clean	`COc1ccc2[nH]cc(CCCC(=O)O)c2c1`
ZINC38813362 ZINC	0.744	232.3 Da LogP 1.81 TPSA 45.3	✓ Ro5	✓ Clean	`COc1ccc2[nH]cc(CC(=O)N(C)C)c2c1`
ZINC209311949 ZINC	0.738	341.4 Da LogP 3.39 TPSA 80.8	✓ Ro5	✓ Clean	`COc1cc(COc2ccc3[nH]cc(CC(=O)O)c3c2)cc(OC)c1`
ZINC71487225 ZINC	0.737	219.2 Da LogP 2.19 TPSA 62.3	✓ Ro5	✓ Clean	`CCOc1ccc2[nH]cc(CC(=O)O)c2c1`
ZINC71631625 ZINC	0.732	281.3 Da LogP 3.47 TPSA 62.3	✓ Ro5	✓ Clean	`COc1cccc(-c2ccc3[nH]cc(CC(=O)O)c3c2)c1`
ZINC685937239 ZINC	0.727	262.3 Da LogP 4.12 TPSA 48.1	✓ Ro5	Alert	`Nc1ccc(Oc2cccc(-c3ccccc3)c2)nc1`
ZINC14455598 ZINC	0.725	233.3 Da LogP 2.28 TPSA 51.3	✓ Ro5	✓ Clean	`CCOC(=O)Cc1c[nH]c2ccc(OC)cc12`
ZINC163194869 ZINC	0.700	233.3 Da LogP 2.58 TPSA 62.3	✓ Ro5	✓ Clean	`CCCOc1ccc2[nH]cc(CC(=O)O)c2c1`
ZINC56406 ZINC	0.690	234.3 Da LogP 1.13 TPSA 88.3	✓ Ro5	✓ Clean	`COc1ccc2[nH]cc(C[C@H](N)C(=O)O)c2c1`
ZINC56407 ZINC	0.690	234.3 Da LogP 1.13 TPSA 88.3	✓ Ro5	✓ Clean	`COc1ccc2[nH]cc(C[C@@H](N)C(=O)O)c2c1`
ZINC138680800 ZINC	0.683	218.3 Da LogP 1.59 TPSA 68.1	✓ Ro5	✓ Clean	`COc1ccc2[nH]cc(CCC(N)=O)c2c1`
ZINC141126474 ZINC	0.683	233.3 Da LogP 2.28 TPSA 51.3	✓ Ro5	✓ Clean	`COC(=O)CCc1c[nH]c2ccc(OC)cc12`
ZINC132921 ZINC	0.679	225.2 Da LogP 2.41 TPSA 52.3	✓ Ro5	✓ Clean	`NC(=O)C1c2ccccc2Oc2ccccc21`
ZINC166484 ZINC	0.677	220.7 Da LogP 3.11 TPSA 48.1	✓ Ro5	Alert	`Nc1ccc(Oc2ccc(Cl)cc2)nc1`
ZINC223106450 ZINC	0.677	202.2 Da LogP 2.16 TPSA 68.4	✓ Ro5	Alert	`Nc1ccc(Oc2ccc(O)cc2)nc1`
ZINC8550321 ZINC	0.677	200.2 Da LogP 2.76 TPSA 48.1	✓ Ro5	Alert	`Cc1ccc(Oc2ccc(N)cn2)cc1`
ZINC92665 ZINC	0.677	265.1 Da LogP 3.22 TPSA 48.1	✓ Ro5	Alert	`Nc1ccc(Oc2ccc(Br)cc2)nc1`
ZINC92676 ZINC	0.677	216.2 Da LogP 2.46 TPSA 57.4	✓ Ro5	Alert	`COc1ccc(Oc2ccc(N)cn2)cc1`
ZINC92681 ZINC	0.677	204.2 Da LogP 2.60 TPSA 48.1	✓ Ro5	Alert	`Nc1ccc(Oc2ccc(F)cc2)nc1`
ZINC26507108 ZINC	0.675	259.2 Da LogP 2.69 TPSA 62.3	✓ Ro5	✓ Clean	`O=C(O)Cc1c[nH]c2ccc(OC(F)(F)F)cc12`
ZINC82299022 ZINC	0.674	244.3 Da LogP 2.00 TPSA 54.1	✓ Ro5	✓ Clean	`COc1ccc2[nH]cc(CC(=O)NC3CC3)c2c1`
ZINC237260588 ZINC	0.674	302.3 Da LogP 1.79 TPSA 82.6	✓ Ro5	✓ Clean	`COc1ccc2[nH]cc(CC(=O)N(CC(=O)O)C3CC3)c2c1`
ZINC22209799 ZINC	0.667	236.3 Da LogP 3.61 TPSA 48.1	✓ Ro5	Alert	`Nc1ccc(Oc2ccc3ccccc3c2)nc1`
ZINC393155 ZINC	0.667	268.3 Da LogP 2.43 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)C1c2ccccc2C(C(=O)O)c2ccccc21`
ZINC71773889 ZINC	0.667	206.1 Da LogP -1.77 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(C[C@H](O)C(=O)O)C[C@H](O)C(=O)O`
ZINC71773890 ZINC	0.667	206.1 Da LogP -1.77 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(C[C@H](O)C(=O)O)C[C@@H](O)C(=O)O`
ZINC71773891 ZINC	0.667	206.1 Da LogP -1.77 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(C[C@@H](O)C(=O)O)C[C@@H](O)C(=O)O`
ZINC252571701 ZINC	0.659	354.4 Da LogP 3.40 TPSA 63.8	✓ Ro5	✓ Clean	`COc1cc(OC)cc(N(C)C(=O)Cc2c[nH]c3ccc(OC)cc23)c1`
ZINC1783593 ZINC	0.652	290.3 Da LogP 1.70 TPSA 91.4	✓ Ro5	✓ Clean	`COc1ccc2[nH]cc(CCNC(=O)CCC(=O)O)c2c1`
ZINC27851951 ZINC	0.651	248.3 Da LogP 1.22 TPSA 77.3	✓ Ro5	✓ Clean	`COC(=O)[C@@H](N)Cc1c[nH]c2ccc(OC)cc12`
ZINC27851958 ZINC	0.651	248.3 Da LogP 1.22 TPSA 77.3	✓ Ro5	✓ Clean	`COC(=O)[C@H](N)Cc1c[nH]c2ccc(OC)cc12`
ZINC519625 ZINC	0.651	248.3 Da LogP 2.07 TPSA 63.3	✓ Ro5	✓ Clean	`COC(=O)NCCc1c[nH]c2ccc(OC)cc12`
ZINC57060 ZINC	0.651	232.3 Da LogP 1.86 TPSA 54.1	✓ Ro5	✓ Clean	`COc1ccc2[nH]cc(CCNC(C)=O)c2c1`
ZINC34493551 ZINC	0.650	237.3 Da LogP 3.77 TPSA 25.0	✓ Ro5	✓ Clean	`COc1ccc2[nH]cc(Cc3ccccc3)c2c1`
ZINC15021050 ZINC	0.647	230.2 Da LogP 2.15 TPSA 85.4	✓ Ro5	Alert	`Nc1ccc(Oc2ccc(C(=O)O)cc2)nc1`
ZINC20278501 ZINC	0.647	265.1 Da LogP 3.22 TPSA 48.1	✓ Ro5	Alert	`Nc1ccc(Oc2cccc(Br)c2)nc1`
ZINC22216030 ZINC	0.647	204.2 Da LogP 2.60 TPSA 48.1	✓ Ro5	Alert	`Nc1ccc(Oc2cccc(F)c2)nc1`
ZINC257708811 ZINC	0.647	202.2 Da LogP 2.16 TPSA 68.4	✓ Ro5	Alert	`Nc1ccc(Oc2cccc(O)c2)nc1`
ZINC316806 ZINC	0.647	216.2 Da LogP 2.46 TPSA 57.4	✓ Ro5	Alert	`COc1cccc(Oc2ccc(N)cn2)c1`
ZINC8701103 ZINC	0.647	200.2 Da LogP 2.76 TPSA 48.1	✓ Ro5	Alert	`Cc1cccc(Oc2ccc(N)cn2)c1`
ZINC910812512 ZINC	0.646	316.4 Da LogP 2.09 TPSA 91.4	✓ Ro5	✓ Clean	`COc1ccc2[nH]cc(CC(=O)NC3CC(CC(=O)O)C3)c2c1`

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 A0A0H3GH05

Pathways

KEGG R03443 BioCyc N-ACETYLGLUTPREDUCT-RXN