Protein target profile

VK055_0143

FAD dependent oxidoreductase family protein

Genome: KpATCC43816 Gene: AIK78771.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GRR7

Export view

Length 423

Pocket druggability 0.934

Direct ligand evidence 0 59 total records

Functional annotation 0 EC 3 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. Second pocket predictor agrees P2Rank predicted binding-site probability 0.99. Structure available AlphaFold DB model + ColabFold model Ligand evidence via structure/bioactivity 9 structural and 0 bioactivity records.

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 (%): 23.148 Lower values reduce human off-target concern.
Human E-value: 7.43e-08
Gut microbiome similarity: 3.3% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 88.889 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Localization

Localization: CytoplasmicMembrane

Structure confidence

ColabFold pLDDT: 93.02 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 0.934

Structure A0A0H3GRR7

Pocket Pocket 2

P2Rank 0.988

Structure A0A0H3GRR7

Pocket Pocket 1

ColabFold model

FPocket 0.453 · Pocket 19

P2Rank 0.993 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 157 / 4744 genomes with a hit

Prevalence 3.3%

Cross-references

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

Sequence

UniProt A0A0H3GRR7

Sequence

Primary amino-acid sequence viewer.

MVGVASAWYLSQAGHDVTVIDRQPGPAEETSAANAGQISPGYAAPWAAPGVPLKAIKWMFQRHAPLAIGLDGTSFQLKWMWQMLRNCDTRHYMENKGRMVRLAEYSRDCLKALRDTTGIQYEGRQGGTLQLFRTAKQYENATRDIAVLEDAGVPYQLLEAKRLAEVEPALAEVSHKLTGGLRLPNDETGDCQLFTTRLAAMAEQAGVTFRFNTAVDALLHEGDRIAGVKCGDEIIKGDAYVMAFGSYSTAMLKGLVDIPVYPLKGYSLTIPIAQEDGAPVSTILDETYKIAITRFDQRIRVGGMAEIVGFNKALLQPRRETLEMVVRDLFPRGGHVEQATFWTGLRPMTPDGTPVVGRTAYKNLWLNTGHGTLGWTMACGSGQLISDLISGRTPAIPYDDLAVARYSPGFTPARPQHLHGAHN

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

3 GO

Gene Ontology (GO)

GO:0019478 The chemical reactions and pathways resulting in the breakdown of D-amino acids, the D-enantiomers of amino acids.
GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
GO:0008718 Catalysis of the reaction: a D-alpha-amino acid + a quinone + H2O = a 2-oxocarboxylate + a quinol + NH4+.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

14 records

Show feature table

Start	End	DB	Term	Name
1	401	Hamap	MF_01202	D-amino acid dehydrogenase [dadA].
1	401	InterPro	IPR023080	D-amino acid dehydrogenase DadA
2	53	Gene3D	G3DSA:3.50.50.60	-
2	53	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
260	350	SUPERFAMILY	SSF54373	FAD-linked reductases, C-terminal domain
125	353	Gene3D	G3DSA:3.30.9.10	-
2	410	SUPERFAMILY	SSF51905	FAD/NAD(P)-binding domain
2	410	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
96	394	Gene3D	G3DSA:3.50.50.60	-
96	394	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
2	405	PANTHER	PTHR13847	SARCOSINE DEHYDROGENASE-RELATED
1	388	Pfam	PF01266	FAD dependent oxidoreductase
1	388	InterPro	IPR006076	FAD dependent oxidoreductase
1	53	FunFam	G3DSA:3.50.50.60:FF:000020	D-amino acid dehydrogenase

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.

Download VMD script Full viewer

Loading 3D structure...

Drag to rotate — click the view, then scroll to zoom.

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 #2

0.934

Likely same site as P2Rank 1 8.0 Å 51 shared residues 82% of smaller site

Unusual size

Show in viewer

Surrounding area

Site 2 FPocket #14

0.23

Unusual size

Show in viewer

Surrounding area

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.988

Likely same site as FPocket 2 8.0 Å 51 shared residues 82% of smaller site

Show in viewer

Surrounding area

Site 2 P2Rank #2

0.394

Show in viewer

Surrounding area

Site 3 P2Rank #3

0.235

Show in viewer

Surrounding area

Site 4 P2Rank #4

0.162

Show in viewer

Surrounding area

Site 5 P2Rank #5

0.144

Show in viewer

Surrounding area

Binding pockets · FPocket

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

Site 1 FPocket #19

0.453

Likely same site as P2Rank 4 5.2 Å 7 shared residues 100% of smaller site

Show in viewer

Surrounding area

Site 2 FPocket #24

0.401

Unusual size

Show in viewer

Surrounding area

Site 3 FPocket #1

0.238

Unusual size

Show in viewer

Surrounding area

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.993

Show in viewer

Surrounding area

Site 2 P2Rank #2

0.206

Show in viewer

Surrounding area

Site 3 P2Rank #3

0.142

Show in viewer

Surrounding area

Site 4 P2Rank #4

0.052

Likely same site as FPocket 19 5.2 Å 7 shared residues 100% of smaller site

Show in viewer

Surrounding area

Site 5 P2Rank #5

0.006

Show in viewer

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_A0A0H3GRR7	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_0143	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.

59 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 9 records from similar proteins

Structural ligands 9 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

AAC PDB via homolog 117.1 Da · LogP -0.79 · TPSA 66.4 Open detail RCSB PDB

B6X PDB via homolog Detail RCSB PDB

DMG PDB via homolog Detail RCSB PDB

FOA PDB via homolog Detail RCSB PDB

FON 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
AAC RCSB PDB	1NG3	O31616	117.1 Da LogP -0.79 TPSA 66.4	✓ Ro5	✓ Clean	`CC(=O)NCC(=O)O`
B6X RCSB PDB	6J39	X5IYZ1	248.3 Da LogP 2.62 TPSA 74.6	✓ Ro5	✓ Clean	`CCCCCC[C@H](CC(=O)O)SCC(=O)O`
DMG RCSB PDB	1VRQ	Q50LF2	103.1 Da LogP -0.37 TPSA 40.5	✓ Ro5	✓ Clean	`CN(C)CC(=O)O`
FOA RCSB PDB	2GAG	Q3ZDR0	112.1 Da LogP 0.98 TPSA 50.4	✓ Ro5	✓ Clean	`c1cc(oc1)C(=O)O`
FON RCSB PDB	1VRQ	Q50LF2	473.4 Da LogP -0.73 TPSA 219.8	1 viol.	✓ Clean	`c1cc(ccc1C(=O)N[C@@H](CCC(=O)O)C(=O)O)NC[C@@H]2…`
GOA RCSB PDB	1RYI	O31616	76.1 Da LogP -0.94 TPSA 57.5	✓ Ro5	✓ Clean	`C(C(=O)O)O`
MTG RCSB PDB	3AD7	Q50LF2	105.1 Da LogP -0.90 TPSA 40.1	✓ Ro5	✓ Clean	`CSCC(=O)[O-]`
PEO RCSB PDB	1NG4	O31616	34.0 Da LogP 0.02 TPSA 40.5	✓ Ro5	✓ Clean	`OO`
PYC RCSB PDB	3AD8	Q50LF2	110.1 Da LogP -0.62 TPSA 55.9	✓ Ro5	✓ Clean	`c1cc([nH]c1)C(=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).

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
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…`
ZINC200768381 ZINC	0.727	344.3 Da LogP -0.08 TPSA 153.4	✓ Ro5	✓ Clean	`Nc1nc(=O)c2c([nH]1)NC[C@@H](CNc1ccc(C(=O)O)cc1)…`
ZINC200768411 ZINC	0.727	344.3 Da LogP -0.08 TPSA 153.4	✓ Ro5	✓ Clean	`Nc1nc(=O)c2c([nH]1)NC[C@H](CNc1ccc(C(=O)O)cc1)N…`
ZINC8628600 ZINC	0.716	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	0.716	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@…`
ZINC8655682 ZINC	0.688	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…`
ZINC85394426 ZINC	0.667	206.2 Da LogP 1.80 TPSA 80.6	✓ Ro5	✓ Clean	`O=C(O)c1ccc(C(=O)c2ccco2)o1`
ZINC8997303 ZINC	0.667	487.5 Da LogP 0.07 TPSA 220.1	1 viol.	✓ Clean	`Nc1nc(O)c2c(n1)NC[C@@H](CNc1ccc(C(=O)N[C@@H](CC…`
ZINC8997304 ZINC	0.667	487.5 Da LogP 0.07 TPSA 220.1	1 viol.	✓ Clean	`Nc1nc(O)c2c(n1)NC[C@@H](CNc1ccc(C(=O)N[C@H](CCC…`
ZINC8997305 ZINC	0.667	487.5 Da LogP 0.07 TPSA 220.1	1 viol.	✓ Clean	`Nc1nc(O)c2c(n1)NC[C@H](CNc1ccc(C(=O)N[C@@H](CCC…`
ZINC8997306 ZINC	0.667	487.5 Da LogP 0.07 TPSA 220.1	1 viol.	✓ Clean	`Nc1nc(O)c2c(n1)NC[C@H](CNc1ccc(C(=O)N[C@H](CCCC…`
ZINC2005305 ZINC	0.658	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	0.658	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	0.658	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	0.658	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…`
ZINC2377216 ZINC	0.633	216.3 Da LogP 2.52 TPSA 74.6	✓ Ro5	✓ Clean	`CCCCCCC(CC(=O)O)CC(=O)O`
ZINC12374887 ZINC	0.630	216.2 Da LogP 2.21 TPSA 67.5	✓ Ro5	✓ Clean	`O=C(O)c1ccc(C(=O)c2ccco2)cc1`
ZINC169748282 ZINC	0.623	471.4 Da LogP -0.26 TPSA 219.8	1 viol.	✓ Clean	`Nc1nc(=O)c2c([nH]1)NC=C(CNc1ccc(C(=O)N[C@@H](CC…`
ZINC1710770 ZINC	0.615	200.2 Da LogP 2.35 TPSA 47.3	✓ Ro5	Alert	`O=C(C(=O)c1ccco1)c1ccccc1`
ZINC8655681 ZINC	0.613	487.5 Da LogP 0.07 TPSA 220.1	1 viol.	✓ Clean	`Nc1nc(O)c2c(n1)NC[C@@H](CCNc1ccc(C(=O)N[C@@H](C…`
ZINC8655685 ZINC	0.613	487.5 Da LogP 0.07 TPSA 220.1	1 viol.	✓ Clean	`Nc1nc(O)c2c(n1)NC[C@H](CCNc1ccc(C(=O)N[C@H](CCC…`
ZINC8667682 ZINC	0.613	487.5 Da LogP 0.07 TPSA 220.1	1 viol.	✓ Clean	`Nc1nc(O)c2c(n1)NC[C@@H](CCNc1ccc(C(=O)N[C@H](CC…`
ZINC223670610 ZINC	0.610	459.5 Da LogP -0.28 TPSA 194.0	1 viol.	✓ Clean	`CN(c1ccc(C(=O)N[C@@H](CCC(=O)O)C(=O)O)cc1)[C@@H…`
ZINC3870062 ZINC	0.610	457.4 Da LogP -0.52 TPSA 194.0	1 viol.	✓ Clean	`Nc1nc(=O)c2c([nH]1)NC[C@H]1CN(c3ccc(C(=O)N[C@H]…`
ZINC1613560 ZINC	0.607	216.2 Da LogP 2.21 TPSA 67.5	✓ Ro5	✓ Clean	`O=C(O)c1ccccc1C(=O)c1ccco1`
ZINC100477623 ZINC	0.600	204.2 Da LogP 2.33 TPSA 60.4	✓ Ro5	✓ Clean	`O=C(CC(=O)c1ccco1)c1ccco1`
ZINC1637602 ZINC	0.600	443.5 Da LogP 0.62 TPSA 187.5	1 viol.	✓ Clean	`Nc1nc(=O)c2c([nH]1)NC[C@@H](CCc1ccc(C(=O)N[C@@H…`
ZINC2392141 ZINC	0.600	214.3 Da LogP 4.24 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCC(CCCCC)CC(=O)O`
ZINC6472822 ZINC	0.600	218.2 Da LogP 2.72 TPSA 60.4	✓ Ro5	✓ Clean	`O=C(CCC(=O)c1ccco1)c1ccco1`
ZINC4228235 ZINC	0.597	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	0.597	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	0.597	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	0.597	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](…`
ZINC2578862 ZINC	0.594	200.3 Da LogP 3.85 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCC[C@H](CC)CC(=O)O`
ZINC59199046 ZINC	0.594	200.3 Da LogP 3.85 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCC[C@@H](CC)CC(=O)O`
ZINC156403 ZINC	0.593	274.3 Da LogP 1.47 TPSA 66.9	✓ Ro5	✓ Clean	`O=C(c1ccco1)N1CCN(C(=O)c2ccco2)CC1`
ZINC8536462 ZINC	0.587	473.4 Da LogP -0.73 TPSA 219.8	1 viol.	✓ Clean	`Nc1nc(=O)c2c([nH]1)NC[C@H](CN(C=O)c1ccc(C(=O)N[…`
ZINC19367002 ZINC	0.579	204.2 Da LogP -0.98 TPSA 81.1	✓ Ro5	✓ Clean	`CN(CCN(C)CC(=O)O)CC(=O)O`
ZINC12496906 ZINC	0.577	457.4 Da LogP 0.22 TPSA 202.8	1 viol.	✓ Clean	`CN1C(CNc2ccc(C(=O)N[C@@H](CCC(=O)O)C(=O)O)cc2)=…`
ZINC983943 ZINC	0.577	360.3 Da LogP 4.16 TPSA 90.6	✓ Ro5	✓ Clean	`O=C(c1cc(C(=O)c2ccco2)cc(C(=O)c2ccco2)c1)c1ccco1`
ZINC106891773 ZINC	0.571	204.2 Da LogP 2.65 TPSA 63.6	✓ Ro5	✓ Clean	`O=C(/C=C(\O)c1ccco1)c1ccco1`
ZINC19364891 ZINC	0.571	204.2 Da LogP -0.98 TPSA 81.1	✓ Ro5	✓ Clean	`CN(C)CCN(CC(=O)O)CC(=O)O`
ZINC49815930 ZINC	0.567	216.2 Da LogP 2.21 TPSA 67.5	✓ Ro5	✓ Clean	`O=C(O)c1cccc(C(=O)c2ccco2)c1`
ZINC100305273 ZINC	0.563	286.5 Da LogP 4.91 TPSA 57.5	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC[C@H](O)CC(=O)O`
ZINC100305277 ZINC	0.563	286.5 Da LogP 4.91 TPSA 57.5	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC[C@@H](O)CC(=O)O`
ZINC32838984 ZINC	0.563	272.4 Da LogP 4.52 TPSA 57.5	✓ Ro5	✓ Clean	`CCCCCCCCCCCCC[C@@H](O)CC(=O)O`
ZINC59658579 ZINC	0.563	214.3 Da LogP 4.24 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCCC[C@@H](C)CC(=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.