KpKP13 Protein target profile

Spermidine synthase

Accession: KP13_01870

Gene: speE AHE46310.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GMP3

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Length 286

Pocket druggability (P2Rank · AlphaFold DB model) 0.939

Direct ligand evidence 0 61 total records

Functional annotation 1 EC 4 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

Independent pocket support: P2Rank + FPocket Both predictors report a high-scoring binding site (P2Rank 0.94, FPocket 0.95). Use the 3D pocket comparison to verify whether they identify the same site. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Strong predicted binding pocket FPocket selected-pocket score 0.95. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.94. Review the complete evidence below

Risks to review

Evidence gaps

No metabolic context No SBML/network-derived reaction evidence is loaded for this protein.

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 (%): 44.0 Lower values reduce human off-target concern.
Human E-value: 3.65e-26
Gut microbiome similarity: 1.7% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 0.0 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 94.89 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) 0.939

Structure A0A0H3GMP3

Pocket Pocket 1

Druggability (FPocket) 0.951

Structure A0A0H3GMP3

Pocket Pocket 1

ColabFold model

P2Rank 0.896 · Pocket 1

FPocket 0.615 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 83 / 4744 genomes with a hit

Prevalence 1.7%

Sequence

Primary amino-acid sequence viewer.

MADNPLWHETLHDHFGQYFSVDNVLYHEKTDHQDLIIFDNRAFGRVMALDGVVQTTERDEFIYHEMMTHVPLLAHGNAKHVLIIGGGDGAMLREASRHRSIETITMVEIDAGVVSFCRQYLPNHNAGAYDDPRFTLVIDDGVNFVNQTTQTFDVIISDCTDPIGPGESLFTSAFYEGCKRCLNPGGIFVAQNGVCFLQQDEAVGSHRKLSHYFRDVSFYQAAIPTYYGGIMTFAWASDNEALRHLSSEIIQARFHKANLTCRYYNPAIHTAAFALPQYLHDALSAP

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 4 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

2.5.1.16

Gene Ontology (GO)

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:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0004766 Catalysis of the reaction: S-adenosylmethioninamine + putrescine = 5'-methylthioadenosine + spermidine.
GO:0008295 The chemical reactions and pathways resulting in the formation of spermidine, N-(3-aminopropyl)-1,4-diaminobutane.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

23 records

Show feature table

Start	End	DB	Term	Name
55	286	FunFam	G3DSA:3.40.50.150:FF:000026	Polyamine aminopropyltransferase
17	241	NCBIfam	NF037959	fused MFS/spermidine synthase
6	57	Pfam	PF17284	Spermidine synthase tetramerisation domain
6	57	InterPro	IPR035246	Spermidine synthase, tetramerisation domain
55	285	Gene3D	G3DSA:3.40.50.150	Vaccinia Virus protein VP39
55	285	InterPro	IPR029063	S-adenosyl-L-methionine-dependent methyltransferase superfamily
60	239	Pfam	PF01564	Spermine/spermidine synthase domain
1	54	Gene3D	G3DSA:2.30.140.10	Spermidine synthase, tetramerisation domain
1	54	InterPro	IPR037163	Spermidine synthase, tetramerisation domain superfamily
81	191	CDD	cd02440	AdoMet_MTases
7	278	NCBIfam	TIGR00417	spermidine synthase
7	278	InterPro	IPR001045	Spermidine/spermine synthases
7	283	SUPERFAMILY	SSF53335	S-adenosyl-L-methionine-dependent methyltransferases
7	283	InterPro	IPR029063	S-adenosyl-L-methionine-dependent methyltransferase superfamily
5	238	ProSiteProfiles	PS51006	Polyamine biosynthesis (PABS) domain profile.
5	238	InterPro	IPR030374	Polyamine biosynthesis domain
81	94	ProSitePatterns	PS01330	Polyamine biosynthesis (PABS) domain signature.
81	94	InterPro	IPR030373	Polyamine biosynthesis domain, conserved site
1	54	FunFam	G3DSA:2.30.140.10:FF:000002	Polyamine aminopropyltransferase
4	283	PANTHER	PTHR11558	SPERMIDINE/SPERMINE SYNTHASE
4	283	InterPro	IPR001045	Spermidine/spermine synthases
6	284	Hamap	MF_00198	Polyamine aminopropyltransferase [speE].
6	284	InterPro	IPR001045	Spermidine/spermine synthases

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

0.939

Likely same site as FPocket 1 3.0 Å 35 shared residues 90% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.015

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Surrounding area

Pocket 3 P2Rank #3

0.015

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Surrounding area

Pocket 4 P2Rank #4

0.011

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Surrounding area

Pocket 5 P2Rank #5

0.011

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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

0.951 Unusual size

Likely same site as P2Rank 1 3.0 Å 35 shared residues 90% of smaller site

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Surrounding area

Residue sets

UniProt: Active site:158-158 Proton acceptor

UniProt: Binding site:108-108

UniProt: Binding site:140-141

UniProt: Binding site:158-161

UniProt: Binding site:165-165

UniProt: Binding site:33-33

UniProt: Binding site:64-64

UniProt: Binding site:88-88

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.896

Likely same site as FPocket 5 1.9 Å 27 shared residues 90% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.584

Likely same site as FPocket 1 3.2 Å 12 shared residues 75% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.057

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Surrounding area

Pocket 4 P2Rank #4

0.035

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Surrounding area

Pocket 5 P2Rank #5

0.012

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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

0.615

Likely same site as P2Rank 2 3.2 Å 12 shared residues 75% of smaller site

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Surrounding area

Pocket 2 FPocket #5

0.443 Unusual size

Likely same site as P2Rank 1 1.9 Å 27 shared residues 90% of smaller site

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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_A0A0H3GMP3	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_01870	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 7 0 loaded crystals

Measured bioactivity 4 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

DSH PDB via homolog 340.4 Da · LogP -0.89 · TPSA 145.3 Open detail RCSB PDB

HAI PDB via homolog Detail RCSB PDB

MLI PDB via homolog Detail RCSB PDB

MTA PDB via homolog Detail RCSB PDB

PUT 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
DSH RCSB PDB	3RW9	P19623	340.4 Da LogP -0.89 TPSA 145.3	✓ Ro5	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
HAI RCSB PDB	6O65	Q9ZUB3	100.2 Da LogP 0.56 TPSA 27.6	✓ Ro5	✓ Clean	`C1CCC(CC1)[NH3+]`
MLI RCSB PDB	6O64	O48661	102.0 Da LogP -3.12 TPSA 80.3	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(=O)[O-]`
MTA RCSB PDB	2O05	P19623	297.3 Da LogP -0.61 TPSA 119.3	✓ Ro5	✓ Clean	`CSC[C@@H]1[C@H]([C@H]([C@@H](O1)n2cnc3c2ncnc3N)…`
PUT RCSB PDB	2O06	P19623	88.2 Da LogP -0.32 TPSA 52.0	✓ Ro5	✓ Clean	`C(CCN)CN`
S4M RCSB PDB	2O0L	P19623	356.5 Da LogP -0.99 TPSA 145.3	✓ Ro5	✓ Clean	`C[S@@H](CCCN)C[C@@H]1[C@H]([C@H]([C@@H](O1)n2cn…`
SPD RCSB PDB	2O07	P19623	145.2 Da LogP -0.34 TPSA 64.1	✓ Ro5	✓ Clean	`C(CCNCCCN)CN`

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
CHEMBL608868 ChEMBL	P19623	8.52 ~3.0 nM	408.5 Da LogP -1.15 TPSA 183.4	2 viol.	✓ Clean	`NCCCCNC(CCN)CC[C@H]1OC(n2cnc3c(N)ncnc32)[C@H](O…`
CHEMBL605227 ChEMBL	P19623	7.70 ~20.0 nM	482.7 Da LogP -0.02 TPSA 183.4	2 viol.	✓ Clean	`NCCCNCCCCCC(CCN)SC[C@H]1OC(n2cnc3c(N)ncnc32)[C@…`
CHEMBL330673 ChEMBL	P19623	6.60 ~251.2 nM	425.6 Da LogP -0.00 TPSA 171.3	1 viol.	✓ Clean	`NCCCCCC(CCN)SC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C…`
CHEMBL2021377 ChEMBL	P19623	6.30 ~501.2 nM	425.6 Da LogP -0.00 TPSA 171.3	1 viol.	✓ Clean	`NCCCCC[C@H](CCN)SC[C@H]1O[C@@H](n2cnc3c(N)ncnc3…`

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
ZINC5487110 ZINC	1.000	425.6 Da LogP -0.00 TPSA 171.3	1 viol.	✓ Clean	`NCCCCC[C@@H](CCN)SC[C@@H]1O[C@H](n2cnc3c(N)ncnc…`
ZINC5487111 ZINC	1.000	425.6 Da LogP -0.00 TPSA 171.3	1 viol.	✓ Clean	`NCCCCC[C@@H](CCN)SC[C@@H]1O[C@@H](n2cnc3c(N)ncn…`
ZINC5487114 ZINC	1.000	425.6 Da LogP -0.00 TPSA 171.3	1 viol.	✓ Clean	`NCCCCC[C@@H](CCN)SC[C@@H]1O[C@H](n2cnc3c(N)ncnc…`
ZINC5487117 ZINC	1.000	425.6 Da LogP -0.00 TPSA 171.3	1 viol.	✓ Clean	`NCCCCC[C@@H](CCN)SC[C@@H]1O[C@@H](n2cnc3c(N)ncn…`
ZINC27564039 ZINC	0.933	202.3 Da LogP -0.36 TPSA 76.1	✓ Ro5	✓ Clean	`NCCCCNCCCNCCCN`
ZINC13377742 ZINC	0.929	230.4 Da LogP 0.42 TPSA 76.1	✓ Ro5	✓ Clean	`NCCCCNCCCCNCCCCN`
ZINC1532734 ZINC	0.929	202.3 Da LogP -0.36 TPSA 76.1	✓ Ro5	✓ Clean	`NCCCNCCCCNCCCN`
ZINC1685531 ZINC	0.875	200.4 Da LogP 2.80 TPSA 52.0	✓ Ro5	✓ Clean	`NCCCCCCCCCCCCN`
ZINC34273707 ZINC	0.875	256.5 Da LogP 4.37 TPSA 52.0	✓ Ro5	✓ Clean	`NCCCCCCCCCCCCCCCCN`
ZINC5178646 ZINC	0.875	228.4 Da LogP 3.59 TPSA 52.0	✓ Ro5	✓ Clean	`NCCCCCCCCCCCCCCN`
ZINC1598087 ZINC	0.867	215.4 Da LogP 1.61 TPSA 64.1	✓ Ro5	✓ Clean	`NCCCCCCNCCCCCCN`
ZINC5163039 ZINC	0.683	340.4 Da LogP -0.89 TPSA 145.3	✓ Ro5	✓ Clean	`NCCCSC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@H](O)[C…`
ZINC100056474 ZINC	0.650	270.5 Da LogP 4.63 TPSA 38.0	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCNCCCN`
ZINC107767463 ZINC	0.650	200.4 Da LogP 2.68 TPSA 38.0	✓ Ro5	✓ Clean	`CCCCCCNCCCCCCN`
ZINC59496006 ZINC	0.650	242.5 Da LogP 3.85 TPSA 38.0	✓ Ro5	✓ Clean	`CCCCCCCCCCCCNCCCN`
ZINC100349915 ZINC	0.627	297.3 Da LogP -0.61 TPSA 119.3	✓ Ro5	✓ Clean	`CSC[C@@H]1O[C@H](n2cnc3c(N)ncnc32)[C@H](O)[C@@H…`
ZINC105279440 ZINC	0.627	297.3 Da LogP -0.61 TPSA 119.3	✓ Ro5	✓ Clean	`CSC[C@H]1O[C@H](n2cnc3c(N)ncnc32)[C@H](O)[C@H]1O`
ZINC12501834 ZINC	0.627	297.3 Da LogP -0.61 TPSA 119.3	✓ Ro5	✓ Clean	`CSC[C@@H]1O[C@H](n2cnc3c(N)ncnc32)[C@@H](O)[C@@…`
ZINC1318753 ZINC	0.627	297.3 Da LogP -0.61 TPSA 119.3	✓ Ro5	✓ Clean	`CSC[C@@H]1O[C@H](n2cnc3c(N)ncnc32)[C@H](O)[C@H]…`
ZINC25963247 ZINC	0.627	297.3 Da LogP -0.61 TPSA 119.3	✓ Ro5	✓ Clean	`CSC[C@H]1O[C@H](n2cnc3c(N)ncnc32)[C@@H](O)[C@H]…`
ZINC3869319 ZINC	0.627	297.3 Da LogP -0.61 TPSA 119.3	✓ Ro5	✓ Clean	`CSC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@@H](O)[C@H…`
ZINC4228245 ZINC	0.627	297.3 Da LogP -0.61 TPSA 119.3	✓ Ro5	✓ Clean	`CSC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@H](O)[C@@H…`
ZINC5929300 ZINC	0.627	297.3 Da LogP -0.61 TPSA 119.3	✓ Ro5	✓ Clean	`CSC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@H](O)[C@H]…`
ZINC895091 ZINC	0.627	297.3 Da LogP -0.61 TPSA 119.3	✓ Ro5	✓ Clean	`CSC[C@@H]1O[C@H](n2cnc3c(N)ncnc32)[C@@H](O)[C@H…`
ZINC73315766 ZINC	0.625	381.5 Da LogP 1.73 TPSA 119.3	✓ Ro5	✓ Clean	`CCCCCCCSC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@@H](…`
ZINC73315769 ZINC	0.625	381.5 Da LogP 1.73 TPSA 119.3	✓ Ro5	✓ Clean	`CCCCCCCSC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@@H]…`
ZINC73315770 ZINC	0.625	381.5 Da LogP 1.73 TPSA 119.3	✓ Ro5	✓ Clean	`CCCCCCCSC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@@H](…`
ZINC73315774 ZINC	0.625	381.5 Da LogP 1.73 TPSA 119.3	✓ Ro5	✓ Clean	`CCCCCCCSC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@@H]…`
ZINC3814316 ZINC	0.614	266.3 Da LogP -2.01 TPSA 145.3	✓ Ro5	✓ Clean	`NC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@H](O)[C@@H]…`
ZINC4773848 ZINC	0.614	266.3 Da LogP -2.01 TPSA 145.3	✓ Ro5	✓ Clean	`NC[C@@H]1O[C@H](n2cnc3c(N)ncnc32)[C@H](O)[C@@H]…`
ZINC4773849 ZINC	0.614	266.3 Da LogP -2.01 TPSA 145.3	✓ Ro5	✓ Clean	`NC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@H](O)[C@@H…`
ZINC4773850 ZINC	0.614	266.3 Da LogP -2.01 TPSA 145.3	✓ Ro5	✓ Clean	`NC[C@@H]1O[C@H](n2cnc3c(N)ncnc32)[C@@H](O)[C@@H…`
ZINC4773851 ZINC	0.614	266.3 Da LogP -2.01 TPSA 145.3	✓ Ro5	✓ Clean	`NC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@@H](O)[C@@…`
ZINC77981211 ZINC	0.614	266.3 Da LogP -2.01 TPSA 145.3	✓ Ro5	✓ Clean	`NC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@@H](O)[C@H]…`
ZINC82228511 ZINC	0.614	266.3 Da LogP -2.01 TPSA 145.3	✓ Ro5	✓ Clean	`NC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@H](O)[C@H]1O`
ZINC14766197 ZINC	0.603	339.4 Da LogP 0.42 TPSA 119.3	✓ Ro5	✓ Clean	`CC(C)CSC[C@@H]1O[C@H](n2cnc3c(N)ncnc32)[C@@H](O…`
ZINC201682330 ZINC	0.603	339.4 Da LogP 0.42 TPSA 119.3	✓ Ro5	✓ Clean	`CC(C)CSC[C@@H]1O[C@H](n2cnc3c(N)ncnc32)[C@H](O)…`
ZINC248157271 ZINC	0.603	339.4 Da LogP 0.42 TPSA 119.3	✓ Ro5	✓ Clean	`CC(C)CSC[C@@H]1O[C@H](n2cnc3c(N)ncnc32)[C@H](O)…`
ZINC2516140 ZINC	0.603	339.4 Da LogP 0.42 TPSA 119.3	✓ Ro5	✓ Clean	`CC(C)CSC[C@@H]1O[C@H](n2cnc3c(N)ncnc32)[C@@H](O…`
ZINC5138266 ZINC	0.603	339.4 Da LogP 0.42 TPSA 119.3	✓ Ro5	✓ Clean	`CC(C)CSC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@H](O)…`
ZINC5139067 ZINC	0.596	283.3 Da LogP -1.04 TPSA 119.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CS)[C@@H](O)[C@H]1O`
ZINC13522378 ZINC	0.594	370.4 Da LogP -1.83 TPSA 182.6	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CSC[C@H](N)C(=O)O)[…`
ZINC13522407 ZINC	0.594	370.4 Da LogP -1.83 TPSA 182.6	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CSC[C@H](N)C(=O)O)[…`
ZINC256828117 ZINC	0.594	370.4 Da LogP -1.83 TPSA 182.6	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CSC[C@H](N)C(=O)O)[…`
ZINC256828118 ZINC	0.594	370.4 Da LogP -1.83 TPSA 182.6	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CSC[C@H](N)C(=O)O)[…`
ZINC1775937521 ZINC	0.592	423.5 Da LogP -1.02 TPSA 194.7	2 viol.	✓ Clean	`CCCN[C@H](CC[C@H](N)C(=O)O)C[C@H]1O[C@@H](n2cnc…`
ZINC95921230 ZINC	0.592	423.5 Da LogP -1.02 TPSA 194.7	2 viol.	✓ Clean	`CCCN[C@@H](CC[C@H](N)C(=O)O)C[C@H]1O[C@@H](n2cn…`
ZINC33821012 ZINC	0.591	384.4 Da LogP -1.44 TPSA 182.6	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CSCC[C@H](N)C(=O)O)…`
ZINC45789230 ZINC	0.591	384.4 Da LogP -1.44 TPSA 182.6	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CSCC[C@H](N)C(=O)O…`
ZINC45789233 ZINC	0.591	384.4 Da LogP -1.44 TPSA 182.6	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CSCC[C@H](N)C(=O)O)[…`

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 A0A0H3GMP3

Chemistry

ChEMBL CHEMBL608868 ChEMBL CHEMBL605227 ChEMBL CHEMBL330673 ChEMBL CHEMBL2021377