KpATCC43816 Protein target profile

methionine aminotransferase, PLP-dependent

Accession: VK055_1888

Gene: AIK80494.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism 6 reactions UniProt A0A0H3GPY3

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Length 386

Pocket druggability (P2Rank · AlphaFold DB model) 0.83

Metabolic reactions 6

Chokepoint No

Direct ligand evidence 0 61 total records

Functional annotation 0 EC 5 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 97.3% of genes in this genome. No isoenzyme backup detected Imported GPR rules do not show an alternative enzyme for the catalyzed reaction set. Second pocket predictor agrees P2Rank predicted binding-site probability 0.83. Structure available AlphaFold DB model + ColabFold model 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: Hit
Human identity (%): 34.247 Lower values reduce human off-target concern.
Human E-value: 9.98e-35
Gut microbiome similarity: 2.4% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 33.245 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 97.23 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) 0.83

Structure A0A0H3GPY3

Pocket Pocket 1

Druggability (FPocket) 0.165

Structure A0A0H3GPY3

Pocket Pocket 9

ColabFold model

P2Rank 0.847 · Pocket 1

FPocket 0.397 · Pocket 1

Core conservation Accessory gene

Roary core

CoreCruncher accessory

Gut microbiome 114 / 4744 genomes with a hit

Prevalence 2.4%

Metabolic context

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

Explore metabolic network

Metabolic context: more central than 97.3% of genes in this genome.

Relative network centrality 97.3% more central than 97.3% of genes in this genome

Chokepoint Not a chokepoint

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MNNNPLIPESKLPALGTTIFTQMSALAQQHQAINLSQGFPDFDGPRYLQERLAYHVAQGANQYAPMTGVPALREAIAGKTADLYGYQPDVNSEITVTAGATEALYAAITALVRRGDEVICFDPSYDSYAPAVALAGGELRRIALQPPHFRVDWRQFAAALSEKTRLVILNTPHNPSATVWQREDFAALWQAIAEREIYVLSDEVYEHICFAEGGHASVLAHPQLRERAVAVSSFGKTFHMTGWKVGYCVAPAAISAELRKVHQYLTFSVNTPAQLAIADMLREAPEHYRELPAFYRERRDLFIEALRPSRLEILPCEGTYFLLADYSAISDLDDVSFCRWLTTEVGVAAIPLSVFCADPFPHKLIRLCFAKQPATLLAAATRLCQL

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

5 GO

Subcellular localization

Localization: Unknown

Gene Ontology (GO)

GO:0009058 A cellular process consisting of the biochemical pathways by which a living organism synthesizes chemical substances. This typically represents the energy-requiring part of metabolism in which simpler substances are transformed into more complex ones.
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:0030170 Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0016212 Catalysis of the reaction: 2-oxoglutarate + L-kynurenine = H2O + kynurenate + L-glutamate. The product 4-(2-aminophenyl)-2,4-dioxobutanoate is converted into kynurenate by a spontaneous reaction. Also acts on 3-hydroxykynurenine to form xanthurenate.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

11 records

Show feature table

Start	End	DB	Term	Name
22	383	Gene3D	G3DSA:3.90.1150.10	Aspartate Aminotransferase, domain 1
22	383	InterPro	IPR015422	Pyridoxal phosphate-dependent transferase, small domain
62	283	FunFam	G3DSA:3.40.640.10:FF:000033	Aspartate aminotransferase
10	385	SUPERFAMILY	SSF53383	PLP-dependent transferases
10	385	InterPro	IPR015424	Pyridoxal phosphate-dependent transferase
45	284	Gene3D	G3DSA:3.40.640.10	-
45	284	InterPro	IPR015421	Pyridoxal phosphate-dependent transferase, major domain
11	385	PANTHER	PTHR43807	FI04487P
33	385	CDD	cd00609	AAT_like
32	382	Pfam	PF00155	Aminotransferase class I and II
32	382	InterPro	IPR004839	Aminotransferase, class I/classII

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

0.83

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Surrounding area

Pocket 2 P2Rank #2

0.067

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Surrounding area

Pocket 3 P2Rank #3

0.038

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Surrounding area

Pocket 4 P2Rank #4

0.03

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Surrounding area

Pocket 5 P2Rank #5

0.02

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Surrounding area

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.847

Likely same site as FPocket 1 1.9 Å 18 shared residues 95% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.202

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Surrounding area

Pocket 3 P2Rank #3

0.008

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Surrounding area

Pocket 4 P2Rank #4

0.007

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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_A0A0H3GPY3	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_1888	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.

61 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 11 records from similar proteins

Structural ligands 8 0 loaded crystals

Measured bioactivity 3 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

C6P PDB via homolog 352.3 Da · LogP 0.18 · TPSA 149.2 Open detail RCSB PDB

HCI PDB via homolog Detail RCSB PDB

IAC PDB via homolog Detail RCSB PDB

IK2 PDB via homolog Detail RCSB PDB

KMT 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
C6P RCSB PDB	2R5C	Q17CS8	352.3 Da LogP 0.18 TPSA 149.2	1 viol.	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CN[C@@H](CS)C(=O)O)O`
HCI RCSB PDB	1V2F	Q75WK2	150.2 Da LogP 1.70 TPSA 37.3	✓ Ro5	✓ Clean	`c1ccc(cc1)CCC(=O)O`
IAC RCSB PDB	3FVU	Q16773	175.2 Da LogP 1.79 TPSA 53.1	✓ Ro5	✓ Clean	`c1ccc2c(c1)c(c[nH]2)CC(=O)O`
IK2 RCSB PDB	4WLJ	Q16773	322.2 Da LogP -0.19 TPSA 158.4	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CNOCC(=O)O)O`
KMT RCSB PDB	1V2E	Q75WK2	148.2 Da LogP 0.39 TPSA 54.4	✓ Ro5	✓ Clean	`CSCCC(=O)C(=O)O`
KYN RCSB PDB	3E2Z	Q71RI9	208.2 Da LogP 0.25 TPSA 106.4	✓ Ro5	✓ Clean	`c1ccc(c(c1)C(=O)C[C@@H](C(=O)O)N)N`
PMP RCSB PDB	3E2Y	Q71RI9	248.2 Da LogP 0.16 TPSA 125.9	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CN)O`
QLP RCSB PDB	2R5E	Q17CS8	377.3 Da LogP -0.49 TPSA 192.3	1 viol.	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CN[C@@H](CCC(=O)N)C(=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).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
DWT ChEMBL	Q6YP21	7.82 ~15.1 nM	503.5 Da LogP 5.75 TPSA 97.6	2 viol.	✓ Clean	`Cc1ccc(cc1Nc2c3cn(nc3nc(n2)c4cccnc4)C)C(=O)Nc5c…`
3IO ChEMBL	Q16773	—	203.2 Da LogP 1.36 TPSA 70.2	✓ Ro5	✓ Clean	`c1ccc2c(c1)c(c[nH]2)CC(=O)C(=O)O`
CHEMBL445966 ChEMBL	Q16773	—	187.2 Da LogP 2.27 TPSA 53.1	✓ Ro5	✓ Clean	`O=C(O)/C=C/c1c[nH]c2ccccc12`

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
ZINC1532617 ZINC	1.000	203.2 Da LogP 1.36 TPSA 70.2	✓ Ro5	✓ Clean	`O=C(O)C(=O)Cc1c[nH]c2ccccc12`
ZINC1532708 ZINC	1.000	248.2 Da LogP 0.16 TPSA 125.9	✓ Ro5	✓ Clean	`Cc1ncc(COP(=O)(O)O)c(CN)c1O`
ZINC895186 ZINC	1.000	208.2 Da LogP 0.25 TPSA 106.4	✓ Ro5	✓ Clean	`Nc1ccccc1C(=O)C[C@H](N)C(=O)O`
ZINC901103 ZINC	1.000	208.2 Da LogP 0.25 TPSA 106.4	✓ Ro5	✓ Clean	`Nc1ccccc1C(=O)C[C@@H](N)C(=O)O`
ZINC406914 ZINC	0.800	222.2 Da LogP 1.72 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCc1ccc(CCC(=O)O)cc1`
ZINC3896921 ZINC	0.788	247.3 Da LogP 4.06 TPSA 32.9	✓ Ro5	✓ Clean	`O=C(/C=C/c1c[nH]c2ccccc12)c1ccccc1`
ZINC4899521 ZINC	0.778	203.2 Da LogP 0.52 TPSA 84.9	✓ Ro5	✓ Clean	`NC(=O)[C@H](N)Cc1c[nH]c2ccccc12`
ZINC57505 ZINC	0.778	203.2 Da LogP 0.52 TPSA 84.9	✓ Ro5	✓ Clean	`NC(=O)[C@@H](N)Cc1c[nH]c2ccccc12`
ZINC1532705 ZINC	0.769	249.2 Da LogP 0.20 TPSA 120.1	✓ Ro5	✓ Clean	`Cc1ncc(COP(=O)(O)O)c(CO)c1O`
ZINC84689016 ZINC	0.767	203.2 Da LogP 1.16 TPSA 70.2	✓ Ro5	✓ Clean	`O=C(O)Cc1c[nH]c2ccccc2c1=O`
ZINC9998612 ZINC	0.750	226.3 Da LogP 3.37 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)CCc1ccc(-c2ccccc2)cc1`
ZINC1690614 ZINC	0.743	233.2 Da LogP 1.50 TPSA 90.4	✓ Ro5	✓ Clean	`O=C(O)C(Cc1c[nH]c2ccccc12)C(=O)O`
ZINC2163727 ZINC	0.739	222.2 Da LogP 1.72 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCc1cccc(CCC(=O)O)c1`
ZINC1637998 ZINC	0.732	261.3 Da LogP 0.24 TPSA 108.2	✓ Ro5	✓ Clean	`N[C@H](Cc1c[nH]c2ccccc12)C(=O)NCC(=O)O`
ZINC2384992 ZINC	0.732	261.3 Da LogP 0.24 TPSA 108.2	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]c2ccccc12)C(=O)NCC(=O)O`
ZINC264238 ZINC	0.732	293.4 Da LogP 2.35 TPSA 70.9	✓ Ro5	✓ Clean	`N[C@H](Cc1c[nH]c2ccccc12)C(=O)NCc1ccccc1`
ZINC264242 ZINC	0.732	293.4 Da LogP 2.35 TPSA 70.9	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]c2ccccc12)C(=O)NCc1ccccc1`
ZINC1673354 ZINC	0.727	238.3 Da LogP 3.82 TPSA 17.1	✓ Ro5	✓ Clean	`O=C(CCc1ccccc1)CCc1ccccc1`
ZINC1693912 ZINC	0.727	266.3 Da LogP 3.39 TPSA 34.1	✓ Ro5	Alert	`O=C(CCc1ccccc1)C(=O)CCc1ccccc1`
ZINC134858 ZINC	0.722	227.3 Da LogP 3.21 TPSA 53.1	✓ Ro5	✓ Clean	`CC(=C/C(=O)O)/C=C/c1c[nH]c2ccccc12`
ZINC4692944 ZINC	0.722	227.3 Da LogP 3.21 TPSA 53.1	✓ Ro5	✓ Clean	`CC(/C=C/c1c[nH]c2ccccc12)=C\C(=O)O`
ZINC79036547 ZINC	0.719	209.2 Da LogP 0.38 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@H](CC(=O)c1ccccc1O)C(=O)O`
ZINC34781219 ZINC	0.718	218.3 Da LogP 1.21 TPSA 68.1	✓ Ro5	✓ Clean	`COC(=O)[C@H](N)Cc1c[nH]c2ccccc12`
ZINC34781220 ZINC	0.718	218.3 Da LogP 1.21 TPSA 68.1	✓ Ro5	✓ Clean	`COC(=O)[C@@H](N)Cc1c[nH]c2ccccc12`
ZINC1557161 ZINC	0.714	390.4 Da LogP 2.33 TPSA 124.0	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@@H](Cc1c[nH]…`
ZINC1557164 ZINC	0.714	390.4 Da LogP 2.33 TPSA 124.0	✓ Ro5	✓ Clean	`N[C@H](Cc1c[nH]c2ccccc12)C(=O)N[C@H](Cc1c[nH]c2…`
ZINC14982898 ZINC	0.711	220.2 Da LogP 0.83 TPSA 99.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]c2c(O)cccc12)C(=O)O`
ZINC14982901 ZINC	0.711	220.2 Da LogP 0.83 TPSA 99.3	✓ Ro5	✓ Clean	`N[C@H](Cc1c[nH]c2c(O)cccc12)C(=O)O`
ZINC193616 ZINC	0.707	279.3 Da LogP 2.68 TPSA 70.9	✓ Ro5	✓ Clean	`N[C@H](Cc1c[nH]c2ccccc12)C(=O)Nc1ccccc1`
ZINC2497690 ZINC	0.707	279.3 Da LogP 2.68 TPSA 70.9	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]c2ccccc12)C(=O)Nc1ccccc1`
ZINC35051054 ZINC	0.707	294.4 Da LogP 2.78 TPSA 68.1	✓ Ro5	✓ Clean	`N[C@H](Cc1c[nH]c2ccccc12)C(=O)OCc1ccccc1`
ZINC35051056 ZINC	0.707	294.4 Da LogP 2.78 TPSA 68.1	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]c2ccccc12)C(=O)OCc1ccccc1`
ZINC874230 ZINC	0.707	231.3 Da LogP 1.17 TPSA 70.9	✓ Ro5	✓ Clean	`CCNC(=O)[C@H](N)Cc1c[nH]c2ccccc12`
ZINC874233 ZINC	0.707	231.3 Da LogP 1.17 TPSA 70.9	✓ Ro5	✓ Clean	`CCNC(=O)[C@@H](N)Cc1c[nH]c2ccccc12`
ZINC57380 ZINC	0.706	232.2 Da LogP 0.91 TPSA 82.2	✓ Ro5	✓ Clean	`O=C(O)CNC(=O)Cc1c[nH]c2ccccc12`
ZINC100795811 ZINC	0.703	289.3 Da LogP 4.35 TPSA 53.1	✓ Ro5	✓ Clean	`O=C(/C=C(\O)c1ccccc1)/C=C/c1c[nH]c2ccccc12`
ZINC103474067 ZINC	0.703	289.3 Da LogP 4.35 TPSA 53.1	✓ Ro5	✓ Clean	`O=C(/C=C/c1c[nH]c2ccccc12)/C=C(/O)c1ccccc1`
ZINC39098 ZINC	0.703	205.2 Da LogP 1.16 TPSA 73.3	✓ Ro5	✓ Clean	`O=C(O)[C@@H](O)Cc1c[nH]c2ccccc12`
ZINC39099 ZINC	0.703	205.2 Da LogP 1.16 TPSA 73.3	✓ Ro5	✓ Clean	`O=C(O)[C@H](O)Cc1c[nH]c2ccccc12`
ZINC83138991 ZINC	0.703	268.1 Da LogP 2.56 TPSA 53.1	✓ Ro5	✓ Clean	`O=C(O)[C@@H](Br)Cc1c[nH]c2ccccc12`
ZINC34307123 ZINC	0.700	217.3 Da LogP 0.78 TPSA 70.9	✓ Ro5	✓ Clean	`CNC(=O)[C@@H](N)Cc1c[nH]c2ccccc12`
ZINC34482181 ZINC	0.700	217.3 Da LogP 0.78 TPSA 70.9	✓ Ro5	✓ Clean	`CNC(=O)[C@H](N)Cc1c[nH]c2ccccc12`
ZINC52968847 ZINC	0.700	232.3 Da LogP 1.60 TPSA 68.1	✓ Ro5	✓ Clean	`CCOC(=O)[C@@H](N)Cc1c[nH]c2ccccc12`
ZINC53943847 ZINC	0.700	232.3 Da LogP 1.60 TPSA 68.1	✓ Ro5	✓ Clean	`CCOC(=O)[C@H](N)Cc1c[nH]c2ccccc12`
ZINC1638007 ZINC	0.698	275.3 Da LogP 0.63 TPSA 108.2	✓ Ro5	✓ Clean	`C[C@H](NC(=O)[C@@H](N)Cc1c[nH]c2ccccc12)C(=O)O`
ZINC205262 ZINC	0.697	264.3 Da LogP 3.03 TPSA 44.9	✓ Ro5	✓ Clean	`O=C(Cc1c[nH]c2ccccc12)NCc1ccccc1`
ZINC57378 ZINC	0.697	203.2 Da LogP 2.58 TPSA 53.1	✓ Ro5	✓ Clean	`O=C(O)CCCc1c[nH]c2ccccc12`
ZINC2557924 ZINC	0.694	239.2 Da LogP 3.31 TPSA 32.9	✓ Ro5	✓ Clean	`O=C(/C=C/c1c[nH]c2ccccc12)C(F)(F)F`
ZINC3163511 ZINC	0.694	213.3 Da LogP 3.41 TPSA 32.9	✓ Ro5	✓ Clean	`CC(C)C(=O)/C=C/c1c[nH]c2ccccc12`
ZINC33376532 ZINC	0.694	239.2 Da LogP 3.31 TPSA 32.9	✓ Ro5	✓ Clean	`O=C(/C=C\c1c[nH]c2ccccc12)C(F)(F)F`

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.

methionine aminotransferase, PLP-dependent

Promising target candidate with multiple supporting evidence streams.

Main supporting evidence

Risks to review

Evidence coverage

Prioritization evidence

Off-target risk

Essentiality

Structure confidence

Binding-site evidence

Metabolic context

Sequence

Functional annotations

Subcellular localization

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · P2Rank

Binding pockets · P2Rank

Binding pockets · FPocket

Structural evidence

Ligand evidence

Cross-references

Sequence

Chemistry

Pathways