Protein target profile

KP13_02102

Delta-aminolevulinic acid dehydratase

Genome: KpKP13 Gene: AHE46102.1 hemB 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GNW5

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Length 324

Pocket druggability 0.454

Direct ligand evidence 0 58 total records

Functional annotation 1 EC 6 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

Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Moderate predicted binding pocket FPocket selected-pocket score 0.45. This supports review but is not experimental validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.59. Structure available AlphaFold DB model + ColabFold model 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 (%): 42.384 Lower values reduce human off-target concern.
Human E-value: 3.93e-76
Gut microbiome similarity: 8.7% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 92.593 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 96.57 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

The selected pocket score is the FPocket value used for ranking after applying the curated structure priority. It estimates small-molecule pocket quality; it is not experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

FPocket 0.454

Structure A0A0H3GNW5

Pocket Pocket 1

P2Rank 0.587

Structure A0A0H3GNW5

Pocket Pocket 1

ColabFold model

FPocket 0.163 · Pocket 4

P2Rank 0.372 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 413 / 4744 genomes with a hit

Prevalence 8.7%

Cross-references

External database identifiers for this protein, its structures, ligands, and metabolic reactions.

Sequence

UniProt A0A0H3GNW5

Chemistry

ChEMBL CHEMBL2430574

Sequence

Primary amino-acid sequence viewer.

MTDLITRPRRLRQSAALRALFEETTLSLNDLVLPIFVEEEIDDYKAIEAMPGVMRIPEKYLAREIERIANAGIRSVMTFGISHHTDATGSDTWNENGLVARMSRICKSTVPEMIVMSDTCFCEYTSHGHCGVLCDHGVDNDATLENLGKQAVVAAAAGADFIAPSAAMDGQVQAIRRSLDAAGFTNTAIMSYSTKFASSFYGPFREAAGTALKGDRKTYQMSPMNRREAIRESLLDEAQGADCLMVKPAGAYLDILRDIRERSDLPLGAYQVSGEYAMIKFAAQAGAIDEEKVVLESLGAIKRAGADLIFSYFALDLAEKKILR

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

4.2.1.24

Gene Ontology (GO)

GO:0033014 The chemical reactions and pathways leading to the formation of tetrapyrroles, natural pigments containing four pyrrole rings joined by one-carbon units linking position 2 of one pyrrole ring to position 5 of the next.
GO:0004655 Catalysis of the reaction: 2 5-aminolevulinate = 2 H2O + H+ + porphobilinogen.
GO:0046872 Binding to a metal ion.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0008270 Binding to a zinc ion (Zn).
GO:0006782 The chemical reactions and pathways resulting in the formation of protoporphyrinogen IX.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

27 records

Show feature table

Start	End	DB	Term	Name
1	323	PIRSF	PIRSF001415	Porphbilin_synth
1	323	InterPro	IPR001731	Delta-aminolevulinic acid dehydratase
4	319	SUPERFAMILY	SSF51569	Aldolase
2	323	FunFam	G3DSA:3.20.20.70:FF:000019	Delta-aminolevulinic acid dehydratase
240	252	ProSitePatterns	PS00169	Delta-aminolevulinic acid dehydratase active site.
240	252	InterPro	IPR030656	Delta-aminolevulinic acid dehydratase, active site
265	280	PRINTS	PR00144	Delta-aminolevulinic acid dehydratase signature
265	280	InterPro	IPR001731	Delta-aminolevulinic acid dehydratase
151	170	PRINTS	PR00144	Delta-aminolevulinic acid dehydratase signature
151	170	InterPro	IPR001731	Delta-aminolevulinic acid dehydratase
295	314	PRINTS	PR00144	Delta-aminolevulinic acid dehydratase signature
295	314	InterPro	IPR001731	Delta-aminolevulinic acid dehydratase
240	256	PRINTS	PR00144	Delta-aminolevulinic acid dehydratase signature
240	256	InterPro	IPR001731	Delta-aminolevulinic acid dehydratase
189	208	PRINTS	PR00144	Delta-aminolevulinic acid dehydratase signature
189	208	InterPro	IPR001731	Delta-aminolevulinic acid dehydratase
121	135	PRINTS	PR00144	Delta-aminolevulinic acid dehydratase signature
121	135	InterPro	IPR001731	Delta-aminolevulinic acid dehydratase
6	319	Pfam	PF00490	Delta-aminolevulinic acid dehydratase
6	319	InterPro	IPR001731	Delta-aminolevulinic acid dehydratase
3	321	SMART	SM01004	ALAD_2
3	321	InterPro	IPR001731	Delta-aminolevulinic acid dehydratase
9	320	CDD	cd00384	ALAD_PBGS
2	324	Gene3D	G3DSA:3.20.20.70	Aldolase class I
2	324	InterPro	IPR013785	Aldolase-type TIM barrel
4	319	PANTHER	PTHR11458	DELTA-AMINOLEVULINIC ACID DEHYDRATASE
4	319	InterPro	IPR001731	Delta-aminolevulinic acid dehydratase

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 · FPocket

Druggability: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Site 1 FPocket #1

0.454

Likely same site as P2Rank 1 1.9 Å 11 shared residues 100% of smaller site

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Surrounding area

Site 2 FPocket #18

0.219

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Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.587

Likely same site as FPocket 1 1.9 Å 11 shared residues 100% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.264

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Surrounding area

Site 3 P2Rank #3

0.158

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Surrounding area

Site 4 P2Rank #4

0.042

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Surrounding area

Site 5 P2Rank #5

0.012

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Surrounding area

Residue sets

UniProt: Active site:195-195 Schiff-base intermediate with substrate

UniProt: Active site:247-247 Schiff-base intermediate with substrate

UniProt: Binding site:120-120

UniProt: Binding site:122-122

UniProt: Binding site:130-130

UniProt: Binding site:205-205

UniProt: Binding site:216-216

UniProt: Binding site:232-232

UniProt: Binding site:273-273

UniProt: Binding site:312-312

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.372

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Surrounding area

Site 2 P2Rank #2

0.214

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Surrounding area

Site 3 P2Rank #3

0.096

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Surrounding area

Site 4 P2Rank #4

0.009

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Surrounding area

Site 5 P2Rank #5

0.009

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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_A0A0H3GNW5	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_02102	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.

58 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 8 records from similar proteins

Structural ligands 7 0 loaded crystals

Measured bioactivity 1 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

4OX PDB via homolog 216.2 Da · LogP 1.46 · TPSA 91.7 Open detail RCSB PDB

AYC PDB via homolog Detail RCSB PDB

DSB PDB via homolog Detail RCSB PDB

LAF PDB via homolog Detail RCSB PDB

PBG 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
4OX RCSB PDB	1L6Y	P0ACB2	216.2 Da LogP 1.46 TPSA 91.7	✓ Ro5	✓ Clean	`C(CCC(=O)CCC(=O)O)CCC(=O)O`
AYC RCSB PDB	2WOQ	Q59643	187.2 Da LogP -0.06 TPSA 83.5	✓ Ro5	✓ Clean	`C[C@H](C(=O)CCC(=O)O)NC(=O)C`
DSB RCSB PDB	1I8J	P0ACB2	230.2 Da LogP 0.63 TPSA 108.7	✓ Ro5	✓ Clean	`C(CC(=O)CCC(=O)O)C(=O)CCC(=O)O`
LAF RCSB PDB	1GZG	Q59643	134.1 Da LogP 0.39 TPSA 54.4	✓ Ro5	✓ Clean	`C(CC(=O)O)C(=O)CF`
PBG RCSB PDB	5MHB	P0ACB2	226.2 Da LogP 0.12 TPSA 116.4	✓ Ro5	✓ Clean	`c1c(c(c([nH]1)CN)CC(=O)O)CCC(=O)O`
PE5 RCSB PDB	2WOQ	Q59643	398.5 Da LogP 0.13 TPSA 94.1	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOCCOCCOCCOCCO`
SHF RCSB PDB	1B4E	P0ACB2	116.1 Da LogP 0.44 TPSA 54.4	✓ Ro5	✓ Clean	`CC(=O)CCC(=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).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
CHEMBL2430574 ChEMBL	P0ACB2	—	473.5 Da LogP 4.84 TPSA 84.2	✓ Ro5	✓ Clean	`O=C(O)c1ccc2c(c1)nc(CCNC(=O)c1cccs1)n2Cc1cccc(C…`

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
ZINC35465466 ZINC	1.000	244.3 Da LogP 2.24 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCC(=O)CCC(=O)O`
ZINC5650743 ZINC	1.000	222.3 Da LogP 0.07 TPSA 57.2	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCO`
ZINC56609 ZINC	1.000	226.2 Da LogP 0.12 TPSA 116.4	✓ Ro5	✓ Clean	`NCc1[nH]cc(CCC(=O)O)c1CC(=O)O`
ZINC6403917 ZINC	1.000	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOCCOCCOCCO`
ZINC26897400 ZINC	0.882	286.4 Da LogP 3.41 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCCC(=O)CCCCCCC(=O)O`
ZINC3074813 ZINC	0.882	258.3 Da LogP 2.63 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCC(=O)CCCCCC(=O)O`
ZINC34423725 ZINC	0.882	342.5 Da LogP 4.97 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCC(=O)CCCCCCCCC(=O)O`
ZINC4822898 ZINC	0.882	272.3 Da LogP 3.02 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCCC(=O)CCCCCC(=O)O`
ZINC4822900 ZINC	0.882	300.4 Da LogP 3.80 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCC(=O)CCCCCC(=O)O`
ZINC3074815 ZINC	0.833	230.3 Da LogP 1.85 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCC(=O)CCCC(=O)O`
ZINC2508031 ZINC	0.824	230.3 Da LogP 1.85 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCC(=O)CCCCC(=O)O`
ZINC4727003 ZINC	0.727	312.4 Da LogP 4.69 TPSA 71.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCC(=O)CCCCCCCC(=O)O`
ZINC59545317 ZINC	0.727	200.3 Da LogP 2.78 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)CCC(=O)O`
ZINC59545320 ZINC	0.727	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCC(=O)CCC(=O)O`
ZINC59545336 ZINC	0.727	214.3 Da LogP 3.17 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCC(=O)CCC(=O)O`
ZINC1703342 ZINC	0.722	202.2 Da LogP 1.07 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCC(=O)CCCC(=O)O`
ZINC113465827 ZINC	0.714	286.4 Da LogP 3.70 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCC(=O)CCCCCCCCCCO`
ZINC1529497 ZINC	0.706	230.3 Da LogP 3.06 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCC(=O)O`
ZINC1531045 ZINC	0.706	202.2 Da LogP 2.28 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCC(=O)O`
ZINC1593115 ZINC	0.706	216.3 Da LogP 2.67 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCC(=O)O`
ZINC1700020 ZINC	0.706	244.3 Da LogP 3.45 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCC(=O)O`
ZINC3860440 ZINC	0.706	258.4 Da LogP 3.84 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCC(=O)O`
ZINC3861298 ZINC	0.706	286.4 Da LogP 4.62 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCCC(=O)O`
ZINC5113062 ZINC	0.706	272.4 Da LogP 4.23 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCC(=O)O`
ZINC33822324 ZINC	0.696	228.3 Da LogP 2.35 TPSA 71.4	✓ Ro5	✓ Clean	`O=CCCC(=O)CCCCCCCC(=O)O`
ZINC12501520 ZINC	0.688	458.5 Da LogP -0.88 TPSA 123.5	1 viol.	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC3874716 ZINC	0.688	414.5 Da LogP -0.90 TPSA 114.3	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC4283769 ZINC	0.688	238.3 Da LogP -0.96 TPSA 77.4	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCO`
ZINC4521548 ZINC	0.688	282.3 Da LogP -0.95 TPSA 86.6	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCO`
ZINC5178829 ZINC	0.688	326.4 Da LogP -0.93 TPSA 95.8	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCO`
ZINC5178830 ZINC	0.688	370.4 Da LogP -0.91 TPSA 105.1	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC5859031 ZINC	0.688	294.4 Da LogP 1.13 TPSA 55.4	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOCCOCC`
ZINC138457918 ZINC	0.682	228.3 Da LogP 3.56 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)CCCCC(=O)O`
ZINC138458029 ZINC	0.682	228.3 Da LogP 3.56 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCCCCC(=O)O`
ZINC144395054 ZINC	0.682	242.4 Da LogP 3.95 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCC(=O)CCCCCCCC(=O)O`
ZINC196749828 ZINC	0.682	214.3 Da LogP 3.17 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCCCC(=O)O`
ZINC2113934076 ZINC	0.682	256.4 Da LogP 4.34 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCCCCCCC(=O)O`
ZINC2113934081 ZINC	0.682	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCC(=O)CCCCCCCCCCC(=O)O`
ZINC2113934082 ZINC	0.682	256.4 Da LogP 4.34 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)CCCCCCC(=O)O`
ZINC2113934083 ZINC	0.682	256.4 Da LogP 4.34 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCC(=O)CCCCC(=O)O`
ZINC2243668 ZINC	0.682	214.3 Da LogP 3.17 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCC(=O)CCCCCCC(=O)O`
ZINC2243670 ZINC	0.682	228.3 Da LogP 3.56 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCC(=O)CCCCCCC(=O)O`
ZINC2378799 ZINC	0.682	200.3 Da LogP 2.78 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCC(=O)CCCCCC(=O)O`
ZINC2378809 ZINC	0.682	200.3 Da LogP 2.78 TPSA 54.4	✓ Ro5	✓ Clean	`CCCC(=O)CCCCCCC(=O)O`
ZINC3074822 ZINC	0.682	229.3 Da LogP 2.11 TPSA 80.4	✓ Ro5	✓ Clean	`NCCCCCC(=O)CCCCCC(=O)O`
ZINC33820423 ZINC	0.682	242.4 Da LogP 3.95 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCC(=O)CCCCCCCCC(=O)O`
ZINC4822737 ZINC	0.682	313.5 Da LogP 4.45 TPSA 80.4	✓ Ro5	✓ Clean	`NCCCCCCCCCCCC(=O)CCCCCC(=O)O`
ZINC5973005 ZINC	0.682	242.4 Da LogP 3.95 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCCCCCC(=O)O`
ZINC79244776 ZINC	0.682	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)CCCCCCCC(=O)O`
ZINC86039283 ZINC	0.682	242.4 Da LogP 3.95 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCC(=O)CCCCC(=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.