KpATCC43816 Protein target profile

5-methyltetrahydropteroyltriglutamate-- homocysteine S-methyltransferase

Accession: VK055_3151

Gene: metE AIK81723.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism 2 reactions UniProt A0A0H3GH70

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Length 754

Pocket druggability (P2Rank · AlphaFold DB model) 0.961

Metabolic reactions 2

Chokepoint Yes

Direct ligand evidence 0 56 total records

Functional annotation 1 EC 6 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. Independent pocket support: P2Rank + FPocket Both predictors report a high-scoring binding site (P2Rank 0.96, FPocket 0.89). Use the 3D pocket comparison to verify whether they identify the same site. Central metabolic position More central than 90.5% 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. 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: 3.9% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 54.915 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

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) 0.961

Structure A0A0H3GH70

Pocket Pocket 1

Druggability (FPocket) 0.894

Structure A0A0H3GH70

Pocket Pocket 38

ColabFold model

P2Rank 0.964 · Pocket 1

FPocket 0.991 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 185 / 4744 genomes with a hit

Prevalence 3.9%

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 Cysteine and methionine metabolism, no isoenzyme backup detected, more central than 90.5% of genes in this genome, no human homolog detected.

Relative network centrality 90.5% more central than 90.5% of genes in this genome

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MTIINHTLGFPRVGLRRELKKAQESYWAGNATREELLAVGRELRARHWEQQKQAGVDLLPVGDFAWYDHVLTTSLLLGNVPARHQNKDGSIDIDTLFRIGRGRAPTGEPAAAAEMTKWFNTNYHYMVPEFVKGQQFKLSWTQLLDEVDEALALGHKIKPVLLGPVTYLWLGKVKGEPFDRLTLLNAILPVYQQVLAELAKRGIDWVQIDEPALVLELPPAWLEAFQPAYDALQGQVKLLLTTYFEGVSDNLATIAALPVQGLHVDLVHGKDDVAELHNRLPAGWLLSAGLINGRNVWRADLTEKYAQIKDLVGKRELWVASSCSLLHSPIDLSVETRLDAEVKSWFAFALQKCGELALLRDALNSGDTAAITEWSAPIQARRHSTRVHNAEVEKRLAAITAQDSQRASPYEVRAQAQRQRFNLPKWPTTTIGSFPQTTEIRGLRLDFKKGNLDASHYRTGIAEHIKQAIVEQERLGLDVLVHGEAERNDMVEYFGEHLDGFIFTQNGWVQSYGSRCVKPPVVIGDVSRPQAITVDWAKYAQSLTDKPVKGMLTGPVTILCWSFPREDVSRETIAKQIALALRDEVADLEAAGIGIIQIDEPALREGLPLKRSDWDAYLQWGVEAFRLNAAVAKDDTQIHTHMCYCEFNDIMDSIAALDADVITIETSRSDMELLESFEAFEYPNEIGPGVYDIHSPNVPSVEWIEALLKKAAQRIPVERLWVNPDCGLKTRGWPETRAALANMVQAARNLRQSA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

2.1.1.14

Gene Ontology (GO)

GO:0003871 Catalysis of the reaction: 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-methionine + tetrahydropteroyltri-L-glutamate.
GO:0008652 The chemical reactions and pathways resulting in the formation of amino acids, organic acids containing one or more amino substituents.
GO:0009086 OBSOLETE. The chemical reactions and pathways resulting in the de novo formation of L-methionine (2-amino-4-(methylthio)butanoic acid), a sulfur-containing, essential amino acid found in peptide linkage in proteins.
GO:0008270 Binding to a zinc ion (Zn).
GO:0071265 The chemical reactions and pathways resulting in the formation of L-methionine, the L-enantiomer of (2S)-2-amino-4-(methylsulfanyl)butanoic acid.
GO:0032259 The process in which a methyl group is covalently attached to a molecule.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

24 records

Show feature table

Start	End	DB	Term	Name
427	748	CDD	cd03311	CIMS_C_terminal_like
427	748	InterPro	IPR002629	Cobalamin-independent methionine synthase MetE, C-terminal/archaeal
4	362	CDD	cd03312	CIMS_N_terminal_like
5	753	PANTHER	PTHR30519	5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE--HOMOCYSTEINE METHYLTRANSFERASE
7	519	Gene3D	G3DSA:3.20.20.210	-
7	519	InterPro	IPR038071	UROD/MetE-like superfamily
391	752	SUPERFAMILY	SSF51726	UROD/MetE-like
391	752	InterPro	IPR038071	UROD/MetE-like superfamily
2	754	PIRSF	PIRSF000382	Met_synth_MetE
2	754	InterPro	IPR006276	Cobalamin-independent methionine synthase
387	751	FunFam	G3DSA:3.20.20.210:FF:000002	5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
5	312	Pfam	PF08267	Cobalamin-independent synthase, N-terminal domain
5	312	InterPro	IPR013215	Cobalamin-independent methionine synthase MetE, N-terminal
7	386	FunFam	G3DSA:3.20.20.210:FF:000003	5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
426	748	Pfam	PF01717	Cobalamin-independent synthase, Catalytic domain
426	748	InterPro	IPR002629	Cobalamin-independent methionine synthase MetE, C-terminal/archaeal
5	389	SUPERFAMILY	SSF51726	UROD/MetE-like
5	389	InterPro	IPR038071	UROD/MetE-like superfamily
384	751	Gene3D	G3DSA:3.20.20.210	-
384	751	InterPro	IPR038071	UROD/MetE-like superfamily
3	753	Hamap	MF_00172	5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase [metE].
3	753	InterPro	IPR006276	Cobalamin-independent methionine synthase
8	752	NCBIfam	TIGR01371	5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase
8	752	InterPro	IPR006276	Cobalamin-independent methionine synthase

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

0.961

Likely same site as FPocket 38 5.9 Å 21 shared residues 91% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.843

Likely same site as FPocket 1 3.8 Å 29 shared residues 94% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.563

Likely same site as FPocket 6 2.7 Å 14 shared residues 100% of smaller site

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Surrounding area

Pocket 4 P2Rank #4

0.456

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Surrounding area

Pocket 5 P2Rank #5

0.42

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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 #38

0.894

Likely same site as P2Rank 1 5.9 Å 21 shared residues 91% of smaller site

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Surrounding area

Pocket 2 FPocket #6

0.468

Likely same site as P2Rank 3 2.7 Å 14 shared residues 100% of smaller site

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Surrounding area

Pocket 3 FPocket #1

0.358 Unusual size

Likely same site as P2Rank 2 3.8 Å 29 shared residues 94% of smaller site

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Surrounding area

Residue sets

UniProt: Active site:694-694 Proton donor

UniProt: Binding site:117-117

UniProt: Binding site:122-122

UniProt: Binding site:17-20

UniProt: Binding site:20-20

UniProt: Binding site:431-433

UniProt: Binding site:484-484

UniProt: Binding site:515-516

UniProt: Binding site:561-561

UniProt: Binding site:599-599

UniProt: Binding site:605-605

UniProt: Binding site:641-641

UniProt: Binding site:643-643

UniProt: Binding site:665-665

UniProt: Binding site:726-726

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.964

Likely same site as FPocket 1 3.2 Å 27 shared residues 96% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.849

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Surrounding area

Pocket 3 P2Rank #3

0.674

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Surrounding area

Pocket 4 P2Rank #4

0.578

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Surrounding area

Pocket 5 P2Rank #5

0.535

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Surrounding area

Residue sets

UniProt: Active site:694-694 Proton donor

UniProt: Binding site:117-117

UniProt: Binding site:122-122

UniProt: Binding site:17-20

UniProt: Binding site:20-20

UniProt: Binding site:431-433

UniProt: Binding site:484-484

UniProt: Binding site:515-516

UniProt: Binding site:561-561

UniProt: Binding site:599-599

UniProt: Binding site:605-605

UniProt: Binding site:641-641

UniProt: Binding site:643-643

UniProt: Binding site:665-665

UniProt: Binding site:726-726

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_A0A0H3GH70	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_3151	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.

56 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 6 records from similar proteins

Structural ligands 6 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

39S PDB via homolog 703.7 Da · LogP -1.58 · TPSA 344.4 Open detail RCSB PDB

C2F PDB via homolog Detail RCSB PDB

HCS PDB via homolog Detail RCSB PDB

MRY PDB via homolog Detail RCSB PDB

MTX 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
39S RCSB PDB	4QQU	P82610	703.7 Da LogP -1.58 TPSA 344.4	3 viol.	✓ Clean	`c1cc(ccc1C(=O)N[C@@H](CCC(=O)N[C@@H](CCC(=O)N[C…`
C2F RCSB PDB	1U1J	O50008	459.5 Da LogP -0.26 TPSA 202.8	1 viol.	✓ Clean	`C[N@@]1[C@H](CNC2=C1C(=O)NC(=N2)N)CNc3ccc(cc3)C…`
HCS RCSB PDB	1U22	O50008	135.2 Da LogP -0.28 TPSA 63.3	✓ Ro5	✓ Clean	`C(CS)[C@@H](C(=O)O)N`
MRY RCSB PDB	1T7L	Q9X112	122.1 Da LogP -2.31 TPSA 80.9	✓ Ro5	✓ Clean	`C([C@H]([C@H](CO)O)O)O`
MTX RCSB PDB	4L6H	P82610	454.4 Da LogP 0.27 TPSA 210.5	✓ Ro5	✓ Clean	`CN(Cc1cnc2c(n1)c(nc(n2)N)N)c3ccc(cc3)C(=O)N[C@@…`
THG RCSB PDB	1U22	O50008	445.4 Da LogP -0.28 TPSA 211.6	1 viol.	✓ Clean	`c1cc(ccc1C(=O)N[C@@H](CCC(=O)O)C(=O)O)NC[C@H]2C…`

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
ZINC2005305 ZINC	1.000	459.5 Da LogP -0.26 TPSA 202.8	1 viol.	✓ Clean	`CN1c2c(nc(N)[nH]c2=O)NC[C@@H]1CNc1ccc(C(=O)N[C@…`
ZINC2572666 ZINC	1.000	459.5 Da LogP -0.26 TPSA 202.8	1 viol.	✓ Clean	`CN1c2c(nc(N)[nH]c2=O)NC[C@H]1CNc1ccc(C(=O)N[C@@…`
ZINC4228266 ZINC	1.000	459.5 Da LogP -0.26 TPSA 202.8	1 viol.	✓ Clean	`CN1c2c(nc(N)[nH]c2=O)NC[C@@H]1CNc1ccc(C(=O)N[C@…`
ZINC4228267 ZINC	1.000	459.5 Da LogP -0.26 TPSA 202.8	1 viol.	✓ Clean	`CN1c2c(nc(N)[nH]c2=O)NC[C@H]1CNc1ccc(C(=O)N[C@H…`
ZINC13604299 ZINC	0.825	439.5 Da LogP 0.14 TPSA 199.3	✓ Ro5	✓ Clean	`CN(Cc1cnc2nc(N)nc(N)c2n1)c1ccc(C(=O)N[C@@H](CCC…`
ZINC13284373 ZINC	0.813	453.5 Da LogP 0.53 TPSA 199.3	✓ Ro5	✓ Clean	`CN(Cc1cnc2nc(N)nc(N)c2n1)c1ccc(C(=O)N[C@@H](CCC…`
ZINC8627939 ZINC	0.813	453.5 Da LogP 0.53 TPSA 199.3	✓ Ro5	✓ Clean	`CN(Cc1cnc2nc(N)nc(N)c2n1)c1ccc(C(=O)N[C@H](CCCC…`
ZINC9212425 ZINC	0.803	473.4 Da LogP -0.73 TPSA 219.8	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N(C=O)[C@@H](CNc1ccc(C(=O)N[…`
ZINC9212426 ZINC	0.803	473.4 Da LogP -0.73 TPSA 219.8	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N(C=O)[C@H](CNc1ccc(C(=O)N[C…`
ZINC9212427 ZINC	0.803	473.4 Da LogP -0.73 TPSA 219.8	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N(C=O)[C@@H](CNc1ccc(C(=O)N[…`
ZINC9212428 ZINC	0.803	473.4 Da LogP -0.73 TPSA 219.8	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N(C=O)[C@H](CNc1ccc(C(=O)N[C…`
ZINC255970296 ZINC	0.794	478.5 Da LogP 0.05 TPSA 226.7	✓ Ro5	Alert	`CN(Cc1cnc2nc(N)nc(N)c2n1)c1ccc(C(=O)N[C@@H](CCC…`
ZINC22062147 ZINC	0.785	482.5 Da LogP 0.45 TPSA 188.5	1 viol.	✓ Clean	`COC(=O)CC[C@H](NC(=O)c1ccc(N(C)Cc2cnc3nc(N)nc(N…`
ZINC1734471 ZINC	0.765	488.9 Da LogP 0.92 TPSA 210.5	✓ Ro5	✓ Clean	`CN(Cc1cnc2nc(N)nc(N)c2n1)c1ccc(C(=O)N[C@@H](CCC…`
ZINC8628726 ZINC	0.765	488.9 Da LogP 0.92 TPSA 210.5	✓ Ro5	✓ Clean	`CN(Cc1cnc2nc(N)nc(N)c2n1)c1ccc(C(=O)N[C@H](CCC(…`
ZINC98207756 ZINC	0.727	330.3 Da LogP 0.39 TPSA 136.4	✓ Ro5	✓ Clean	`CN1c2c(nc(N)[nH]c2=O)NC[C@@H]1CNc1ccc(C(=O)O)cc1`
ZINC1560410190 ZINC	0.712	453.4 Da LogP 0.43 TPSA 210.5	✓ Ro5	✓ Clean	`CN(Cc1cnc2nc(N)nc(N)c2n1)c1ccc(C(=O)N[C](CCC(=O…`
ZINC8655682 ZINC	0.711	487.5 Da LogP -0.34 TPSA 219.8	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N(C=O)[C@@H](CCNc1ccc(C(=O)N…`
ZINC4228235 ZINC	0.708	445.4 Da LogP -0.28 TPSA 211.6	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N[C@H](CNc1ccc(C(=O)N[C@@H](…`
ZINC4228236 ZINC	0.708	445.4 Da LogP -0.28 TPSA 211.6	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N[C@H](CNc1ccc(C(=O)N[C@H](C…`
ZINC4228237 ZINC	0.708	445.4 Da LogP -0.28 TPSA 211.6	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N[C@@H](CNc1ccc(C(=O)N[C@@H]…`
ZINC4228238 ZINC	0.708	445.4 Da LogP -0.28 TPSA 211.6	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N[C@@H](CNc1ccc(C(=O)N[C@H](…`
ZINC404265 ZINC	0.683	325.3 Da LogP 0.92 TPSA 144.1	✓ Ro5	✓ Clean	`CN(Cc1cnc2nc(N)nc(N)c2n1)c1ccc(C(=O)O)cc1`
ZINC8628600 ZINC	0.671	473.5 Da LogP 0.13 TPSA 202.8	1 viol.	✓ Clean	`CN1c2c([nH]c(N)nc2=O)NC[C@@H]1CCNc1ccc(C(=O)N[C…`
ZINC8628601 ZINC	0.671	473.5 Da LogP 0.13 TPSA 202.8	1 viol.	✓ Clean	`CN1c2c([nH]c(N)nc2=O)NC[C@H]1CCNc1ccc(C(=O)N[C@…`
ZINC1720422 ZINC	0.651	339.4 Da LogP 1.01 TPSA 133.1	✓ Ro5	✓ Clean	`COC(=O)c1ccc(N(C)Cc2cnc3nc(N)nc(N)c3n2)cc1`
ZINC4228243 ZINC	0.645	457.4 Da LogP -0.52 TPSA 194.0	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N1CN(c3ccc(C(=O)N[C@@H](CCC(…`
ZINC4228244 ZINC	0.645	457.4 Da LogP -0.52 TPSA 194.0	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N1CN(c3ccc(C(=O)N[C@H](CCC(=…`
ZINC4654260 ZINC	0.645	457.4 Da LogP -0.52 TPSA 194.0	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N1CN(c3ccc(C(=O)N[C@@H](CCC(…`
ZINC8618631 ZINC	0.645	459.5 Da LogP 0.11 TPSA 211.6	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N[C@H](CCNc1ccc(C(=O)N[C@@H]…`
ZINC8627114 ZINC	0.645	459.5 Da LogP 0.11 TPSA 211.6	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N[C@@H](CCNc1ccc(C(=O)N[C@@H…`
ZINC4654270 ZINC	0.632	471.4 Da LogP -0.36 TPSA 211.0	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N1C(=O)N(c3ccc(C(=O)N[C@@H](…`
ZINC4654271 ZINC	0.632	471.4 Da LogP -0.36 TPSA 211.0	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N1C(=O)N(c3ccc(C(=O)N[C@@H](…`
ZINC3055005 ZINC	0.619	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	0.619	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	0.619	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC100055463 ZINC	0.615	212.2 Da LogP -4.22 TPSA 141.6	1 viol.	✓ Clean	`OC[C@H](O)[C@@H](O)[C@H](O)[C@H](O)[C@H](O)CO`
ZINC100064885 ZINC	0.615	212.2 Da LogP -4.22 TPSA 141.6	1 viol.	✓ Clean	`OC[C@H](O)[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO`
ZINC1653968 ZINC	0.615	353.4 Da LogP 1.40 TPSA 133.1	✓ Ro5	✓ Clean	`CCOC(=O)c1ccc(N(C)Cc2cnc3nc(N)nc(N)c3n2)cc1`
ZINC17780060 ZINC	0.615	212.2 Da LogP -4.22 TPSA 141.6	1 viol.	✓ Clean	`OC[C@@H](O)[C@H](O)C(O)[C@H](O)[C@H](O)CO`
ZINC17952732 ZINC	0.615	212.2 Da LogP -4.22 TPSA 141.6	1 viol.	✓ Clean	`OC[C@H](O)[C@@H](O)C(O)[C@H](O)[C@H](O)CO`
ZINC18042331 ZINC	0.615	242.2 Da LogP -4.86 TPSA 161.8	1 viol.	✓ Clean	`OC[C@H](O)[C@H](O)[C@H](O)[C@H](O)[C@H](O)[C@H]…`
ZINC18120313 ZINC	0.615	212.2 Da LogP -4.22 TPSA 141.6	1 viol.	✓ Clean	`OC[C@H](O)[C@H](O)C(O)[C@H](O)[C@H](O)CO`
ZINC3979006 ZINC	0.615	212.2 Da LogP -4.22 TPSA 141.6	1 viol.	✓ Clean	`OC[C@@H](O)[C@@H](O)C(O)[C@H](O)[C@H](O)CO`
ZINC4403103 ZINC	0.615	242.2 Da LogP -4.86 TPSA 161.8	1 viol.	✓ Clean	`OC[C@@H](O)[C@H](O)[C@H](O)[C@H](O)[C@H](O)[C@H…`
ZINC4403105 ZINC	0.615	242.2 Da LogP -4.86 TPSA 161.8	1 viol.	✓ Clean	`OC[C@H](O)[C@@H](O)[C@H](O)[C@H](O)[C@H](O)[C@H…`
ZINC4403107 ZINC	0.615	242.2 Da LogP -4.86 TPSA 161.8	1 viol.	✓ Clean	`OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)[C@H](O)[C@…`
ZINC9212412 ZINC	0.615	212.2 Da LogP -4.22 TPSA 141.6	1 viol.	✓ Clean	`OC[C@H](O)[C@@H](O)C(O)[C@H](O)[C@@H](O)CO`
ZINC4228265 ZINC	0.605	443.4 Da LogP 0.01 TPSA 211.9	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N=C(CNc1ccc(C(=O)N[C@@H](CCC…`
ZINC4658144 ZINC	0.605	443.5 Da LogP 0.62 TPSA 187.5	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)C[C@@H](CCc1ccc(C(=O)N[C@H](…`

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 A0A0H3GH70

Pathways

KEGG R04405 BioCyc HOMOCYSMET-RXN KEGG R09365 BioCyc RXN-12730