KpKP13 Protein target profile

Aldehyde dehydrogenase domain-containing protein

Accession: KP13_02304

Gene: AHE42875.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3H299

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Length 450

Pocket druggability (P2Rank · AlphaFold DB model) 0.821

Direct ligand evidence 0 68 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

Independent pocket support: P2Rank + FPocket Both predictors report a high-scoring binding site (P2Rank 0.82, FPocket 0.72). Use the 3D pocket comparison to verify whether they identify the same site. No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. Strong predicted binding pocket FPocket selected-pocket score 0.72. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.82. 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: No hit
Gut microbiome similarity: 1.0% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 44.0 Higher values support similarity to known essential genes.
DEG E-value: 0.008 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 94.31 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) 0.821

Structure A0A0H3H299

Pocket Pocket 1

Druggability (FPocket) 0.719

Structure A0A0H3H299

Pocket Pocket 8

ColabFold model

P2Rank 0.931 · Pocket 1

FPocket 0.551 · Pocket 30

Core conservation Accessory gene

Roary accessory

CoreCruncher accessory

Gut microbiome 47 / 4744 genomes with a hit

Prevalence 1.0%

Sequence

Primary amino-acid sequence viewer.

MSEAIVPLSSIDAAEIRERVRAAGVVGAGGAGFPTHIKLQARVDTVLVNAAECEPMLKVDQQLMAQQADRLIRGLGYAMTATGAREGIIALKAKYAPAIAVLTPRLPEWARLHILPDVYPAGDEVLTIWLATGRRVPPAALPVSVGVVVNNVQTVLNIARAVEQGYPVTRRTLTVNGAVARPLTLAVPLGISLREVLDLAGGATVDDPGFINGGPMMGSLITSLETPVTKTTGGLLVLPGNHPLIQRRRQDERTLLAIARTVCEQCRLCTDLCPRHLIGHELSPHLLVRAVNYRQAATPSLLLSALTCSECNVCESVACPVGISPMRINRLLKRELRAKNLRYDGPLRPADEMAKHRLVPVKRLISKLGLDPWYQEAPLTAVEPEVACVTLPLRQHIGISAVPCVAPGERVTRGQVLADIPADALGAPVHASIDGLVSTITEQAITLVRG

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

5 GO

Subcellular localization

Localization: Cytoplasmic

Gene Ontology (GO)

GO:0009055 A molecular function representing the directed movement of electrons from one molecular entity to another, typically mediated by electron carriers or acceptors, resulting in the transfer of energy and/or the reduction-oxidation (redox) transformation of chemical species. This activity is fundamental to various biological processes, including cellular respiration and photosynthesis, as well as numerous enzymatic reactions involved in metabolic pathways.
GO:0051539 Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands.
GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
GO:0051536 Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms.
GO:0046872 Binding to a metal ion.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

22 records

Show feature table

Start	End	DB	Term	Name
25	167	Gene3D	G3DSA:3.40.50.11540	-
25	167	InterPro	IPR037225	NADH-ubiquinone oxidoreductase 51kDa subunit, FMN-binding domain superfamily
171	239	SUPERFAMILY	SSF142984	Nqo1 middle domain-like
168	235	Gene3D	G3DSA:3.10.20.600	-
263	323	Pfam	PF13534	4Fe-4S dicluster domain
240	344	Gene3D	G3DSA:1.10.1060.10	-
240	344	InterPro	IPR009051	Alpha-helical ferredoxin
213	340	SUPERFAMILY	SSF46548	alpha-helical ferredoxin
9	177	SUPERFAMILY	SSF142019	Nqo1 FMN-binding domain-like
9	177	InterPro	IPR037225	NADH-ubiquinone oxidoreductase 51kDa subunit, FMN-binding domain superfamily
20	159	Pfam	PF01512	Respiratory-chain NADH dehydrogenase 51 Kd subunit
20	159	InterPro	IPR011538	NADH-ubiquinone oxidoreductase 51kDa subunit, FMN-binding domain
11	449	PIRSF	PIRSF036408	PduS
11	449	InterPro	IPR017054	Cobalamin reductase PduS
8	369	PANTHER	PTHR43034	ION-TRANSLOCATING OXIDOREDUCTASE COMPLEX SUBUNIT C
8	369	InterPro	IPR010208	Ion-translocating oxidoreductase complex, subunit RnfC/RsxC
388	446	Pfam	PF13375	RnfC Barrel sandwich hybrid domain
388	446	InterPro	IPR026902	RnfC Barrel sandwich hybrid domain
254	283	ProSiteProfiles	PS51379	4Fe-4S ferredoxin-type iron-sulfur binding domain profile.
254	283	InterPro	IPR017896	4Fe-4S ferredoxin-type, iron-sulphur binding domain
174	218	Pfam	PF10531	SLBB domain
174	218	InterPro	IPR019554	Soluble ligand binding 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

0.821

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Surrounding area

Pocket 2 P2Rank #2

0.408

Likely same site as FPocket 8 3.5 Å 12 shared residues 100% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.27

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Surrounding area

Pocket 4 P2Rank #4

0.102

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Surrounding area

Pocket 5 P2Rank #5

0.049

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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 #8

0.719

Likely same site as P2Rank 2 3.5 Å 12 shared residues 100% of smaller site

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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

0.931

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Surrounding area

Pocket 2 P2Rank #2

0.275

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Surrounding area

Pocket 3 P2Rank #3

0.04

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Surrounding area

Pocket 4 P2Rank #4

0.04

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Surrounding area

Pocket 5 P2Rank #5

0.031

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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_A0A0H3H299	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_02304	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.

68 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 18 records from similar proteins

Structural ligands 18 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

3PE PDB via homolog 748.1 Da · LogP 12.06 · TPSA 134.4 Open detail RCSB PDB

970 PDB via homolog Detail RCSB PDB

AYA PDB via homolog Detail RCSB PDB

CDL PDB via homolog Detail RCSB PDB

DCQ 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
3PE RCSB PDB	6QC2	W5PUX0	748.1 Da LogP 12.06 TPSA 134.4	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](COP(=O)(O)OCCN)OC…`
970 RCSB PDB	6ZKL	W5PUX0	394.4 Da LogP 3.70 TPSA 63.2	✓ Ro5	✓ Clean	`CC(=C)[C@H]1Cc2c(ccc3c2O[C@@H]4COc5cc(c(cc5[C@@…`
AYA RCSB PDB	6ZKL	W5PUX0	131.1 Da LogP -0.40 TPSA 66.4	✓ Ro5	✓ Clean	`C[C@@H](C(=O)O)NC(=O)C`
CDL RCSB PDB	6QC2	W5PUX0	1464.1 Da LogP 23.31 TPSA 242.6	3 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](COP(=O)([O-])OCC(…`
DCQ RCSB PDB	6ZKC	W5PUX0	322.4 Da LogP 4.49 TPSA 52.6	✓ Ro5	Alert	`CCCCCCCCCCC1=C(C(=O)C(=C(C1=O)OC)OC)C`
EHZ RCSB PDB	6G2J	Q91YT0	584.7 Da LogP 3.04 TPSA 182.5	2 viol.	✓ Clean	`CCCCCCCCCCC[C@@H](CC(=O)SCCNC(=O)CCNC(=O)[C@@H]…`
FES RCSB PDB	7Q5Y	O66841	175.8 Da LogP 1.29 TPSA 0.0	✓ Ro5	✓ Clean	`S1[Fe]S[Fe]1`
FME RCSB PDB	6ZKL	W5PUX0	177.2 Da LogP -0.06 TPSA 66.4	✓ Ro5	✓ Clean	`CSCC[C@@H](C(=O)O)NC=O`
HQH RCSB PDB	6Q8O	Q56222	415.6 Da LogP 5.05 TPSA 71.6	1 viol.	✓ Clean	`C/C=C(\C)/[C@@H]([C@H](C)/C=C(\C)/C=C/C/C(=C/CC…`
HQK RCSB PDB	6Q8X	Q56222	364.9 Da LogP 5.24 TPSA 34.9	1 viol.	✓ Clean	`CC(C)(C)c1ccc(cc1)CSC2=C(C(=O)N(N=C2)C(C)(C)C)Cl`
HQW RCSB PDB	6Q8W	Q56222	397.4 Da LogP 4.66 TPSA 91.8	✓ Ro5	✓ Clean	`CC1=C(OC(=C(C1=O)C)OC)[C@H]2C/C(=C/C(=C/c3ccc(c…`
L3W RCSB PDB	6SAQ	O66841	697.4 Da LogP -3.38 TPSA 354.9	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
MYR RCSB PDB	6ZKF	W5PUX0	228.4 Da LogP 4.77 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)O`
PC1 RCSB PDB	6ZKU	W5PUX0	790.2 Da LogP 12.17 TPSA 111.2	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](CO[P@@](=O)([O-])…`
PNS RCSB PDB	5LNK	W5PUX0	358.4 Da LogP -0.96 TPSA 145.2	1 viol.	✓ Clean	`CC(C)(COP(=O)(O)O)[C@H](C(=O)NCCC(=O)NCCS)O`
SMA RCSB PDB	2YBB	Q56222	514.7 Da LogP 6.14 TPSA 87.4	2 viol.	✓ Clean	`C/C=C(\C)/C=C/C=C[C@@H]([C@@H](C)[C@H]([C@@H](C…`
UQ1 RCSB PDB	2YBB	Q56222	250.3 Da LogP 2.32 TPSA 52.6	✓ Ro5	Alert	`CC1=C(C(=O)C(=C(C1=O)OC)OC)CC=C(C)C`
ZMP RCSB PDB	5LNK	W5PUX0	568.7 Da LogP 4.07 TPSA 162.3	1 viol.	✓ Clean	`CCCCCCCCCCCCCC(=O)SCCNC(=O)CCNC(=O)[C@H](C(C)(C…`

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
ZINC13522091 ZINC	1.000	394.4 Da LogP 3.70 TPSA 63.2	✓ Ro5	✓ Clean	`C=C(C)[C@@H]1Cc2c(ccc3c2O[C@@H]2COc4cc(OC)c(OC)…`
ZINC1529498 ZINC	1.000	200.3 Da LogP 3.99 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)O`
ZINC1530417 ZINC	1.000	228.4 Da LogP 4.77 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)O`
ZINC1530836 ZINC	1.000	394.4 Da LogP 3.70 TPSA 63.2	✓ Ro5	✓ Clean	`C=C(C)[C@@H]1Cc2c(ccc3c2O[C@H]2COc4cc(OC)c(OC)c…`
ZINC1559692 ZINC	1.000	250.3 Da LogP 2.32 TPSA 52.6	✓ Ro5	Alert	`COC1=C(OC)C(=O)C(CC=C(C)C)=C(C)C1=O`
ZINC1628119 ZINC	1.000	214.3 Da LogP 4.38 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCC(=O)O`
ZINC2105913 ZINC	1.000	397.4 Da LogP 4.66 TPSA 91.8	✓ Ro5	✓ Clean	`COc1oc([C@@H]2C/C(=C/C(C)=C/c3ccc([N+](=O)[O-])…`
ZINC2548962 ZINC	1.000	394.4 Da LogP 3.70 TPSA 63.2	✓ Ro5	✓ Clean	`C=C(C)[C@@H]1Cc2c(ccc3c2O[C@H]2COc4cc(OC)c(OC)c…`
ZINC2575028 ZINC	1.000	322.4 Da LogP 4.49 TPSA 52.6	✓ Ro5	Alert	`CCCCCCCCCCC1=C(C)C(=O)C(OC)=C(OC)C1=O`
ZINC3860715 ZINC	1.000	394.4 Da LogP 3.70 TPSA 63.2	✓ Ro5	✓ Clean	`C=C(C)[C@H]1Cc2c(ccc3c2O[C@@H]2COc4cc(OC)c(OC)c…`
ZINC3874884 ZINC	1.000	394.4 Da LogP 3.70 TPSA 63.2	✓ Ro5	✓ Clean	`C=C(C)[C@@H]1Cc2c(ccc3c2O[C@@H]2COc4cc(OC)c(OC)…`
ZINC3874885 ZINC	1.000	394.4 Da LogP 3.70 TPSA 63.2	✓ Ro5	✓ Clean	`C=C(C)[C@H]1Cc2c(ccc3c2O[C@H]2COc4cc(OC)c(OC)cc…`
ZINC4025640 ZINC	1.000	397.4 Da LogP 4.66 TPSA 91.8	✓ Ro5	✓ Clean	`COc1oc([C@H]2C/C(=C/C(C)=C/c3ccc([N+](=O)[O-])c…`
ZINC8660420 ZINC	1.000	394.4 Da LogP 3.70 TPSA 63.2	✓ Ro5	✓ Clean	`C=C(C)[C@H]1Cc2c(ccc3c2O[C@@H]2COc4cc(OC)c(OC)c…`
ZINC226792912 ZINC	0.860	396.4 Da LogP 2.72 TPSA 80.3	✓ Ro5	✓ Clean	`COc1cc2c(cc1OC)[C@@H]1C(=O)c3ccc4c(c3O[C@@H]1CO…`
ZINC226792928 ZINC	0.860	396.4 Da LogP 2.72 TPSA 80.3	✓ Ro5	✓ Clean	`COc1cc2c(cc1OC)[C@@H]1C(=O)c3ccc4c(c3O[C@H]1CO2…`
ZINC230121190 ZINC	0.860	396.4 Da LogP 2.72 TPSA 80.3	✓ Ro5	✓ Clean	`COc1cc2c(cc1OC)[C@@H]1C(=O)c3ccc4c(c3O[C@@H]1CO…`
ZINC230121201 ZINC	0.860	396.4 Da LogP 2.72 TPSA 80.3	✓ Ro5	✓ Clean	`COc1cc2c(cc1OC)[C@@H]1C(=O)c3ccc4c(c3O[C@H]1CO2…`
ZINC138457918 ZINC	0.850	228.3 Da LogP 3.56 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)CCCCC(=O)O`
ZINC138458029 ZINC	0.850	228.3 Da LogP 3.56 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCCCCC(=O)O`
ZINC144395054 ZINC	0.850	242.4 Da LogP 3.95 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCC(=O)CCCCCCCC(=O)O`
ZINC14619628 ZINC	0.850	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCC(=O)CCCCCCCCCC(=O)O`
ZINC196749828 ZINC	0.850	214.3 Da LogP 3.17 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCCCC(=O)O`
ZINC2113934076 ZINC	0.850	256.4 Da LogP 4.34 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCCCCCCC(=O)O`
ZINC2113934082 ZINC	0.850	256.4 Da LogP 4.34 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)CCCCCCC(=O)O`
ZINC2113934083 ZINC	0.850	256.4 Da LogP 4.34 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCC(=O)CCCCC(=O)O`
ZINC2243670 ZINC	0.850	228.3 Da LogP 3.56 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCC(=O)CCCCCCC(=O)O`
ZINC2569203 ZINC	0.850	214.3 Da LogP 3.17 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCC(=O)CCCCCC(=O)O`
ZINC4798470 ZINC	0.850	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCCCCCCCC(=O)O`
ZINC5973005 ZINC	0.850	242.4 Da LogP 3.95 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCCCCCC(=O)O`
ZINC71418182 ZINC	0.850	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCCC(=O)CCCCC(=O)O`
ZINC79244776 ZINC	0.850	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)CCCCCCCC(=O)O`
ZINC86037082 ZINC	0.850	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCC(=O)CCCCCC(=O)O`
ZINC86037089 ZINC	0.850	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCC(=O)CCCCCCC(=O)O`
ZINC86039283 ZINC	0.850	242.4 Da LogP 3.95 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCC(=O)CCCCC(=O)O`
ZINC13813085 ZINC	0.820	410.4 Da LogP 2.68 TPSA 83.5	✓ Ro5	✓ Clean	`C=C(CO)[C@@H]1Cc2c(ccc3c2O[C@H]2COc4cc(OC)c(OC)…`
ZINC13813088 ZINC	0.820	410.4 Da LogP 2.68 TPSA 83.5	✓ Ro5	✓ Clean	`C=C(CO)[C@@H]1Cc2c(ccc3c2O[C@@H]2COc4cc(OC)c(OC…`
ZINC2115043 ZINC	0.820	410.4 Da LogP 2.68 TPSA 83.5	✓ Ro5	✓ Clean	`C=C(CO)[C@@H]1Cc2c(ccc3c2O[C@@H]2COc4cc(OC)c(OC…`
ZINC36387001 ZINC	0.820	410.4 Da LogP 2.68 TPSA 83.5	✓ Ro5	✓ Clean	`C=C(CO)[C@@H]1Cc2c(ccc3c2O[C@H]2COc4cc(OC)c(OC)…`
ZINC3947515 ZINC	0.820	410.4 Da LogP 2.68 TPSA 83.5	✓ Ro5	✓ Clean	`C=C(CO)[C@H]1Cc2c(ccc3c2O[C@@H]2COc4cc(OC)c(OC)…`
ZINC2242696 ZINC	0.810	273.3 Da LogP -1.39 TPSA 124.6	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](C)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C…`
ZINC2566274 ZINC	0.810	344.4 Da LogP -1.89 TPSA 153.7	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](C)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C…`
ZINC2572098 ZINC	0.810	202.2 Da LogP -0.90 TPSA 95.5	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](C)C(=O)N[C@@H](C)C(=O)O`
ZINC3160730 ZINC	0.810	214.3 Da LogP 3.17 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)CCCC(=O)O`
ZINC4582907 ZINC	0.810	200.3 Da LogP 2.78 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCCC(=O)O`
ZINC4727003 ZINC	0.810	312.4 Da LogP 4.69 TPSA 71.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCC(=O)CCCCCCCC(=O)O`
ZINC5706638 ZINC	0.810	344.4 Da LogP -1.89 TPSA 153.7	✓ Ro5	✓ Clean	`CC(=O)N[C@H](C)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C(…`
ZINC5706639 ZINC	0.810	344.4 Da LogP -1.89 TPSA 153.7	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](C)C(=O)N[C@H](C)C(=O)N[C@@H](C)C(…`
ZINC5706640 ZINC	0.810	344.4 Da LogP -1.89 TPSA 153.7	✓ Ro5	✓ Clean	`CC(=O)N[C@H](C)C(=O)N[C@H](C)C(=O)N[C@@H](C)C(=…`
ZINC86037074 ZINC	0.810	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)CCCC(=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 A0A0H3H299