KpATCC43816 Protein target profile

aspartate kinase, monofunctional class

Accession: VK055_3062

Gene: AIK81647.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism 1 reaction UniProt A0A0H3GQ40

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Length 449

Pocket druggability (P2Rank · AlphaFold DB model) 0.732

Metabolic reactions 1

Chokepoint No

Direct ligand evidence 0 51 total records

Functional annotation 1 EC 7 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 97.0% 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 0.73. 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: 3.3% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 65.0 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 92.45 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) 0.732

Structure A0A0H3GQ40

Pocket Pocket 1

Druggability (FPocket) 0.596

Structure A0A0H3GQ40

Pocket Pocket 1

ColabFold model

P2Rank 0.805 · Pocket 1

FPocket 0.736 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 155 / 4744 genomes with a hit

Prevalence 3.3%

Metabolic context

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

Explore metabolic network

Metabolic context: more central than 97.0% of genes in this genome, no human homolog detected.

Relative network centrality 97.0% more central than 97.0% of genes in this genome

Chokepoint Not a chokepoint

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MTDLVVAKFGGTSVADFDAMNRSIDVALLDANTRIVVLSASAGVTNILVALAGGLEPTERFSQLDALRQIQFNILERLRYPNVIREEIERLLENITTLAEAAALASSTALTDELVSHGELMSTLLFVEILRERGIQAQWFDARKVLRTNDRFGRAEPDIAAVAELTQQQLAPRLAEGLVVTQGFIGSEAKGRTTTLGRGGSDYTAALLGEALNATRVDIWTDVPGIYTTDPRVAPAAKRIDVIAFEEAAEMATFGAKVLHPATLLPAVRSDIPVFVGSSKEPKAGGTLVCKTTENPPLFRALALRRRQTLLTLHSLNMLHSRGFLAEVFGILARHNISVDLITTSEVSVALTMDTTGSTSAGDTLLTQALLTELSSLCRVEVEENLALVALIGNELSKACGVGKEVFGVLEPFNIRMICYGASSHNLCFLVPGDDAEKVVQKLHHNLFE

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

2.7.2.4

Gene Ontology (GO)

GO:0008652 The chemical reactions and pathways resulting in the formation of amino acids, organic acids containing one or more amino substituents.
GO:0004072 Catalysis of the reaction: L-aspartate + ATP = 4-phospho-L-aspartate + ADP + H+.
GO:0009089 OBSOLETE. The chemical reactions and pathways resulting in the formation of lysine, via the intermediate diaminopimelate.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0009090 The chemical reactions and pathways resulting in the formation of homoserine, alpha-amino-gamma-hydroxybutyric acid.
GO:0009088 The chemical reactions and pathways resulting in the formation of L-threonine (2-amino-3-hydroxybutyric acid), a polar, uncharged, essential amino acid found in peptide linkage in proteins.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

33 records

Show feature table

Start	End	DB	Term	Name
4	277	Pfam	PF00696	Amino acid kinase family
4	277	InterPro	IPR001048	Aspartate/glutamate/uridylate kinase
6	14	ProSitePatterns	PS00324	Aspartokinase signature.
6	14	InterPro	IPR018042	Aspartate kinase, conserved site
313	394	ProSiteProfiles	PS51671	ACT domain profile.
313	394	InterPro	IPR002912	ACT domain
1	449	PANTHER	PTHR21499	ASPARTATE KINASE
4	290	CDD	cd04258	AAK_AKiii-LysC-EC
4	290	InterPro	IPR041745	Lysine-sensitive aspartokinase 3, N-terminal catalytic domain
3	449	NCBIfam	TIGR00657	aspartate kinase
3	449	InterPro	IPR001341	Aspartate kinase
2	449	PIRSF	PIRSF000726	Asp_kin
2	449	InterPro	IPR005260	Aspartate kinase, monofunctional class
4	291	SUPERFAMILY	SSF53633	Carbamate kinase-like
4	291	InterPro	IPR036393	Acetylglutamate kinase-like superfamily
309	379	FunFam	G3DSA:3.30.70.260:FF:000017	Aspartokinase
386	449	CDD	cd04917	ACT_AKiii-LysC-EC_2
309	383	Gene3D	G3DSA:3.30.70.260	-
380	448	FunFam	G3DSA:3.30.70.260:FF:000023	Aspartokinase
323	377	Pfam	PF01842	ACT domain
323	377	InterPro	IPR002912	ACT domain
301	448	Gene3D	G3DSA:3.30.70.260	-
377	448	SUPERFAMILY	SSF55021	ACT-like
377	448	InterPro	IPR045865	ACT-like domain
308	384	CDD	cd04932	ACT_AKiii-LysC-EC_1
42	134	Gene3D	G3DSA:1.20.120.1320	Aspartokinase, catalytic domain
42	134	InterPro	IPR042199	Aspartokinase/Bifunctional aspartokinase/homoserine dehydrogenase, catalytic domain
3	449	NCBIfam	TIGR00656	aspartate kinase, monofunctional class
3	449	InterPro	IPR005260	Aspartate kinase, monofunctional class
6	289	Gene3D	G3DSA:3.40.1160.10	-
6	289	InterPro	IPR036393	Acetylglutamate kinase-like superfamily
297	393	SUPERFAMILY	SSF55021	ACT-like
297	393	InterPro	IPR045865	ACT-like domain

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

0.732

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Surrounding area

Pocket 2 P2Rank #2

0.175

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Surrounding area

Pocket 3 P2Rank #3

0.135

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Surrounding area

Pocket 4 P2Rank #4

0.045

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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

0.596 Unusual size

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Surrounding area

Residue sets

UniProt: Binding site:119-119

UniProt: Binding site:221-222

UniProt: Binding site:227-227

UniProt: Binding site:232-232

UniProt: Binding site:257-258

UniProt: Binding site:45-45

UniProt: Binding site:8-11

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.805

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Surrounding area

Pocket 2 P2Rank #2

0.152

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Surrounding area

Pocket 3 P2Rank #3

0.012

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Surrounding area

Pocket 4 P2Rank #4

0.004

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Surrounding area

Residue sets

UniProt: Binding site:119-119

UniProt: Binding site:221-222

UniProt: Binding site:227-227

UniProt: Binding site:232-232

UniProt: Binding site:257-258

UniProt: Binding site:45-45

UniProt: Binding site:8-11

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_A0A0H3GQ40	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_3062	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.

51 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 1 records from similar proteins

Structural ligands 1 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

TAR PDB via homolog 150.1 Da · LogP -2.12 · TPSA 115.1 Open detail RCSB PDB

ZINC1709621 ZINC proposed compound · Tanimoto 0.600 Detail ZINC

ZINC1709622 ZINC proposed compound · Tanimoto 0.600 Detail ZINC

ZINC1709623 ZINC proposed compound · Tanimoto 0.600 Detail ZINC

ZINC1709624 ZINC proposed compound · Tanimoto 0.600 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
TAR RCSB PDB	2CDQ	Q9LYU8	150.1 Da LogP -2.12 TPSA 115.1	✓ Ro5	✓ Clean	`[C@H]([C@@H](C(=O)O)O)(C(=O)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
ZINC1709621 ZINC	0.600	248.2 Da LogP -2.17 TPSA 167.0	✓ Ro5	✓ Clean	`N[C@@H](CC(=O)N[C@@H](CC(=O)O)C(=O)O)C(=O)O`
ZINC1709622 ZINC	0.600	248.2 Da LogP -2.17 TPSA 167.0	✓ Ro5	✓ Clean	`N[C@H](CC(=O)N[C@@H](CC(=O)O)C(=O)O)C(=O)O`
ZINC1709623 ZINC	0.600	248.2 Da LogP -2.17 TPSA 167.0	✓ Ro5	✓ Clean	`N[C@@H](CC(=O)N[C@H](CC(=O)O)C(=O)O)C(=O)O`
ZINC1709624 ZINC	0.600	248.2 Da LogP -2.17 TPSA 167.0	✓ Ro5	✓ Clean	`N[C@H](CC(=O)N[C@H](CC(=O)O)C(=O)O)C(=O)O`
ZINC1560405156 ZINC	0.588	208.1 Da LogP -1.79 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)/C(O)=C(\O)[C@H](O)[C@H](O)C(=O)O`
ZINC1560405157 ZINC	0.588	208.1 Da LogP -1.79 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)/C(O)=C(/O)[C@H](O)[C@H](O)C(=O)O`
ZINC1575288 ZINC	0.560	248.2 Da LogP -2.17 TPSA 167.0	✓ Ro5	✓ Clean	`N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)O`
ZINC1575289 ZINC	0.560	248.2 Da LogP -2.17 TPSA 167.0	✓ Ro5	✓ Clean	`N[C@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)O`
ZINC1575290 ZINC	0.560	248.2 Da LogP -2.17 TPSA 167.0	✓ Ro5	✓ Clean	`N[C@@H](CC(=O)O)C(=O)N[C@H](CC(=O)O)C(=O)O`
ZINC1575291 ZINC	0.560	248.2 Da LogP -2.17 TPSA 167.0	✓ Ro5	✓ Clean	`N[C@H](CC(=O)O)C(=O)N[C@H](CC(=O)O)C(=O)O`
ZINC5131760 ZINC	0.560	237.2 Da LogP -0.94 TPSA 137.9	✓ Ro5	✓ Clean	`N[C@@H](CS[C@@H](CC(=O)O)C(=O)O)C(=O)O`
ZINC5131761 ZINC	0.560	237.2 Da LogP -0.94 TPSA 137.9	✓ Ro5	✓ Clean	`N[C@H](CS[C@@H](CC(=O)O)C(=O)O)C(=O)O`
ZINC5131922 ZINC	0.560	237.2 Da LogP -0.94 TPSA 137.9	✓ Ro5	✓ Clean	`N[C@@H](CS[C@H](CC(=O)O)C(=O)O)C(=O)O`
ZINC5131923 ZINC	0.560	237.2 Da LogP -0.94 TPSA 137.9	✓ Ro5	✓ Clean	`N[C@H](CS[C@H](CC(=O)O)C(=O)O)C(=O)O`
ZINC2123927 ZINC	0.538	204.2 Da LogP -1.62 TPSA 129.7	✓ Ro5	✓ Clean	`C[C@H](NC(=O)[C@@H](N)CC(=O)O)C(=O)O`
ZINC2560978 ZINC	0.538	204.2 Da LogP -1.62 TPSA 129.7	✓ Ro5	✓ Clean	`C[C@H](NC(=O)C[C@H](N)C(=O)O)C(=O)O`
ZINC1730666 ZINC	0.524	208.2 Da LogP -1.46 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CSC[C@H](N)C(=O)O)C(=O)O`
ZINC1730667 ZINC	0.524	208.2 Da LogP -1.46 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CSC[C@H](N)C(=O)O)C(=O)O`
ZINC1730669 ZINC	0.524	208.2 Da LogP -1.46 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CSC[C@@H](N)C(=O)O)C(=O)O`
ZINC3055005 ZINC	0.524	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCC[C@H](N)C(=O)O)C(=O)O`
ZINC3055007 ZINC	0.524	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC3055010 ZINC	0.524	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC100655912 ZINC	0.519	478.4 Da LogP -4.25 TPSA 299.8	1 viol.	✓ Clean	`N[C@H](CC(=O)O)C(=O)N[C@H](CC(=O)O)C(=O)N[C@H](…`
ZINC100655916 ZINC	0.519	478.4 Da LogP -4.25 TPSA 299.8	1 viol.	✓ Clean	`N[C@H](CC(=O)O)C(=O)N[C@H](CC(=O)O)C(=O)N[C@@H]…`
ZINC255993703 ZINC	0.519	478.4 Da LogP -4.25 TPSA 299.8	1 viol.	✓ Clean	`N[C@H](CC(=O)O)C(=O)N[C@H](CC(=O)O)C(=O)N[C@H](…`
ZINC2568071 ZINC	0.519	218.3 Da LogP -1.08 TPSA 112.7	✓ Ro5	✓ Clean	`CC(C)[C@H](NC(=O)[C@@H](N)[C@@H](C)O)C(=O)O`
ZINC4533843 ZINC	0.519	363.3 Da LogP -3.21 TPSA 233.4	1 viol.	✓ Clean	`N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@…`
ZINC4533848 ZINC	0.519	478.4 Da LogP -4.25 TPSA 299.8	1 viol.	✓ Clean	`N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@…`
ZINC4533853 ZINC	0.519	478.4 Da LogP -4.25 TPSA 299.8	1 viol.	✓ Clean	`N[C@H](CC(=O)O)C(=O)N[C@H](CC(=O)O)C(=O)N[C@@H]…`
ZINC1529331 ZINC	0.500	206.1 Da LogP -2.21 TPSA 149.2	✓ Ro5	✓ Clean	`O=C(O)C(=O)[C@H](C(=O)O)[C@@H](O)C(=O)O`
ZINC1529332 ZINC	0.500	206.1 Da LogP -2.21 TPSA 149.2	✓ Ro5	✓ Clean	`O=C(O)C(=O)[C@H](C(=O)O)[C@H](O)C(=O)O`
ZINC1529333 ZINC	0.500	206.1 Da LogP -2.21 TPSA 149.2	✓ Ro5	✓ Clean	`O=C(O)C(=O)[C@@H](C(=O)O)[C@@H](O)C(=O)O`
ZINC1529334 ZINC	0.500	206.1 Da LogP -2.21 TPSA 149.2	✓ Ro5	✓ Clean	`O=C(O)C(=O)[C@@H](C(=O)O)[C@H](O)C(=O)O`
ZINC1577651 ZINC	0.500	234.2 Da LogP -0.66 TPSA 149.2	✓ Ro5	✓ Clean	`O=C(O)C[C@H](C(=O)O)[C@@H](CC(=O)O)C(=O)O`
ZINC1577652 ZINC	0.500	234.2 Da LogP -0.66 TPSA 149.2	✓ Ro5	✓ Clean	`O=C(O)C[C@@H](C(=O)O)[C@@H](CC(=O)O)C(=O)O`
ZINC1577653 ZINC	0.500	234.2 Da LogP -0.66 TPSA 149.2	✓ Ro5	✓ Clean	`O=C(O)C[C@H](C(=O)O)[C@H](CC(=O)O)C(=O)O`
ZINC1720127 ZINC	0.500	218.3 Da LogP -0.24 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCC[C@H](N)C(=O)O)C(=O)O`
ZINC1720128 ZINC	0.500	218.3 Da LogP -0.24 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC1720130 ZINC	0.500	218.3 Da LogP -0.24 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC22923898 ZINC	0.500	307.3 Da LogP -3.04 TPSA 199.3	1 viol.	✓ Clean	`N[C@@H](CN[C@@H](CN[C@@H](CC(=O)O)C(=O)O)C(=O)O…`
ZINC22930737 ZINC	0.500	307.3 Da LogP -3.04 TPSA 199.3	1 viol.	✓ Clean	`N[C@H](CN[C@H](CN[C@@H](CC(=O)O)C(=O)O)C(=O)O)C…`
ZINC23355305 ZINC	0.500	307.3 Da LogP -3.04 TPSA 199.3	1 viol.	✓ Clean	`N[C@H](CN[C@@H](CN[C@@H](CC(=O)O)C(=O)O)C(=O)O)…`
ZINC2384839 ZINC	0.500	232.2 Da LogP -0.99 TPSA 129.7	✓ Ro5	✓ Clean	`CC(C)[C@H](NC(=O)[C@@H](N)CC(=O)O)C(=O)O`
ZINC2560328 ZINC	0.500	239.1 Da LogP 1.53 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](CC(C(F)(F)F)C(F)(F)F)C(=O)O`
ZINC2561115 ZINC	0.500	321.3 Da LogP -3.49 TPSA 182.2	1 viol.	✓ Clean	`C[C@@H](O)[C@H](N)C(=O)N[C@H](C(=O)N[C@H](C(=O)…`
ZINC4348166 ZINC	0.500	239.1 Da LogP 1.53 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](CC(C(F)(F)F)C(F)(F)F)C(=O)O`
ZINC4580676 ZINC	0.500	202.2 Da LogP -0.85 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](C/C=C/C[C@@H](N)C(=O)O)C(=O)O`
ZINC5462352 ZINC	0.500	321.3 Da LogP -3.49 TPSA 182.2	1 viol.	✓ Clean	`C[C@H](O)[C@H](N)C(=O)N[C@H](C(=O)N[C@H](C(=O)O…`
ZINC5462358 ZINC	0.500	321.3 Da LogP -3.49 TPSA 182.2	1 viol.	✓ Clean	`C[C@H](O)[C@@H](N)C(=O)N[C@H](C(=O)N[C@H](C(=O)…`
ZINC5462362 ZINC	0.500	321.3 Da LogP -3.49 TPSA 182.2	1 viol.	✓ Clean	`C[C@@H](O)[C@H](NC(=O)[C@@H](NC(=O)[C@H](N)[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 A0A0H3GQ40

Pathways

KEGG R00480 BioCyc ASPARTATEKIN-RXN