Protein profile

PA4812

formate dehydrogenase-O major subunit

Genome: NC_002516.2

Gene: PA4812 fdnG Structure source: AlphaFold UniProt Q14T72

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Amino acids 1026

Annotations 13

Features 39

PDB binders 10

Druggability 0.564

Overview

Basic information about this protein and its source genome.

Accession: PA4812
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA4812 fdnG
Status: annotated
Amino acids: 1026
Structure source: AlphaFold

GO:0009326 An enzyme complex that catalyzes the dehydrogenation of formate to produce carbon dioxide (CO2). GO:0042597 The region between the inner (cytoplasmic) and outer membrane (Gram-negative Bacteria) or cytoplasmic membrane and cell wall (Fungi and Gram-positive Bacteria). 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: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:0047111 Catalysis of the reaction: ferricytochrome C-553 + formate = ferrocytochrome C-553 + CO2. GO:0008863 Catalysis of the reaction: formate + NAD+ = CO2 + NADH.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Gut microbiome off-target: hit
Essential (DEG): N
Localization: Periplasmic

Selected Druggability evidence

Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.

FPocket 0.564

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MDMNRRQFFKVCGIGLGGSSLAALGMAPTEAFADQVRHFKLAHTVETRNTCTYCSVGCGLIMYSQGDGAKNVAQNIIHIEGDADHPVNRGTLCPKGAGLLDYIHSPNRLKYPEVREAGSSEWKRIEWDEALERIAKLMKEDRDANFVEKNEQGQTVNRWLTTGFLAASASSNEAGYITHKVMRSLGILGFDNQARVUHGPTVASLAPTFGRGAMTNHWTDIKNADLVLIMGGNAAEAHPCGFKWVTEAKAHNKARLLVVDPRFTRSASVADYYAPIRTGTDIAFLGGLINYLLENDKIQHEYVRNYTDVSFIVKEGFSFEDGLFNGYDAEKRTYPDKSSWGYEIGEDGYAKVDPTLTHPRCVFNLLKQHYSRYTPDVVSNICGTPKDMMLKVWAEIAETSKPGKVMTIMYALGWTQHSVGAQMIRTGAMVQLLLGNIGMPGGGMNALRGHSNIQGLTDLGLLSNSLPGYLTLAMDAEQDYDAYIAKRTAKPLRPGQLSYWQNYGKFHVSLMKAWFGKSATKENNWCYDWLPKLDMPGAGYDVLRYFDMMYQGKVNGYFCQGFNPIASFPNKAKVGAALARLKWMVVMDPLVTETSEFWRNVGEYNDVDTASIKTTVFRLPTSCFAEEDGSIVNSGRWLQWHWKGAEPPGQARPDIAIMAGLFHRLREMYRKDGGAFPDPILGLDWSYLKPDEPGPDELAREFNGKALSDLVDPANGMILAKAGEQLPGFALLRDDGSTASGCWIFAGSWTQQGNQMGRRDNSDPYGMGQTLGWAWAWPANRRILYNRASADVSGKPWDPEKKRLVWWNGKSWGGTDVPDYKADVPPEAGMNPFIMNPEGVARLFAVDKMAEGPFPEHYEPFETPIGVNPLHRDNRKAISNPAARVFKNDMELFGTADEFPYAATTYRLTEHFHYWTKHCRLNAITQPEQFVEIGEALAKELGINAGDKVKVSSNRGYIKAVAVVTKRIRPLQVDGKTVHHVGIPIHWGFAGMARNGFLANTLTPFVGDGNTQTPEFKSFLVNVEKA

MDMNRRQFFKVCGIGLGGSSLAALGMAPTEAFADQVRHFKLAHTVETRNTCTYCSVGCGLIMYSQGDGAKNVAQNIIHIEGDADHPVNRGTLCPKGAGLLDYIHSPNRLKYPEVREAGSSEWKRIEWDEALERIAKLMKEDRDANFVEKNEQGQTVNRWLTTGFLAASASSNEAGYITHKVMRSLGILGFDNQARVUHGPTVASLAPTFGRGAMTNHWTDIKNADLVLIMGGNAAEAHPCGFKWVTEAKAHNKARLLVVDPRFTRSASVADYYAPIRTGTDIAFLGGLINYLLENDKIQHEYVRNYTDVSFIVKEGFSFEDGLFNGYDAEKRTYPDKSSWGYEIGEDGYAKVDPTLTHPRCVFNLLKQHYSRYTPDVVSNICGTPKDMMLKVWAEIAETSKPGKVMTIMYALGWTQHSVGAQMIRTGAMVQLLLGNIGMPGGGMNALRGHSNIQGLTDLGLLSNSLPGYLTLAMDAEQDYDAYIAKRTAKPLRPGQLSYWQNYGKFHVSLMKAWFGKSATKENNWCYDWLPKLDMPGAGYDVLRYFDMMYQGKVNGYFCQGFNPIASFPNKAKVGAALARLKWMVVMDPLVTETSEFWRNVGEYNDVDTASIKTTVFRLPTSCFAEEDGSIVNSGRWLQWHWKGAEPPGQARPDIAIMAGLFHRLREMYRKDGGAFPDPILGLDWSYLKPDEPGPDELAREFNGKALSDLVDPANGMILAKAGEQLPGFALLRDDGSTASGCWIFAGSWTQQGNQMGRRDNSDPYGMGQTLGWAWAWPANRRILYNRASADVSGKPWDPEKKRLVWWNGKSWGGTDVPDYKADVPPEAGMNPFIMNPEGVARLFAVDKMAEGPFPEHYEPFETPIGVNPLHRDNRKAISNPAARVFKNDMELFGTADEFPYAATTYRLTEHFHYWTKHCRLNAITQPEQFVEIGEALAKELGINAGDKVKVSSNRGYIKAVAVVTKRIRPLQVDGKTVHHVGIPIHWGFAGMARNGFLANTLTPFVGDGNTQTPEFKSFLVNVEKA

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

13 GO

Gene Ontology (GO)

GO:0009326 An enzyme complex that catalyzes the dehydrogenation of formate to produce carbon dioxide (CO2).
GO:0042597 The region between the inner (cytoplasmic) and outer membrane (Gram-negative Bacteria) or cytoplasmic membrane and cell wall (Fungi and Gram-positive Bacteria).
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: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:0047111 Catalysis of the reaction: ferricytochrome C-553 + formate = ferrocytochrome C-553 + CO2.
GO:0008863 Catalysis of the reaction: formate + NAD+ = CO2 + NADH.
GO:0036397 Catalysis of the reaction: formate + a quinone = CO2 + a quinol.
GO:0046872 Binding to a metal ion.
GO:0043546 Binding to a molybdopterin cofactor (Moco), essential for the catalytic activity of some enzymes, e.g. sulfite oxidase, xanthine dehydrogenase, and aldehyde oxidase. The cofactor consists of a mononuclear molybdenum (Mo-molybdopterin) or tungsten ion (W-molybdopterin) coordinated by one or two molybdopterin ligands.
GO:0009061 The enzymatic release of energy from inorganic and organic compounds (especially carbohydrates and fats) which uses compounds other than oxygen (e.g. nitrate, sulfate) as the terminal electron acceptor.
GO:0015944 The chemical reactions and pathways by which formate is converted to CO2.
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:0045333 The enzymatic release of energy from inorganic and organic compounds (especially carbohydrates and fats) which either requires oxygen (aerobic respiration) or does not (anaerobic respiration).

Sequence Features

Domain/signature hits from InterPro and related databases.

39 records

Show feature table

Start	End	DB	Term	Name
108	595	Pfam	PF00384	Molybdopterin oxidoreductase
108	595	InterPro	IPR006656	Molybdopterin oxidoreductase
519	687	FunFam	G3DSA:3.40.50.740:FF:000007	Formate dehydrogenase, alpha subunit, selenocysteine-containing
37	858	SUPERFAMILY	SSF53706	Formate dehydrogenase/DMSO reductase, domains 1-3
903	1019	Pfam	PF01568	Molydopterin dinucleotide binding domain
903	1019	InterPro	IPR006657	Molybdopterin dinucleotide-binding domain
44	107	ProSiteProfiles	PS51669	Prokaryotic molybdopterin oxidoreductases 4Fe-4S domain profile.
44	107	InterPro	IPR006963	Molybdopterin oxidoreductase, 4Fe-4S domain
49	67	ProSitePatterns	PS00551	Prokaryotic molybdopterin oxidoreductases signature 1.
49	67	InterPro	IPR027467	Molybdopterin oxidoreductase, molybdopterin cofactor binding site
25	33	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
765	847	FunFam	G3DSA:3.40.228.10:FF:000009	Formate dehydrogenase, alpha subunit, selenocysteine-containing
1	1026	PANTHER	PTHR43598	TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B
848	1026	Gene3D	G3DSA:2.40.40.20	-
46	104	Pfam	PF04879	Molybdopterin oxidoreductase Fe4S4 domain
46	104	InterPro	IPR006963	Molybdopterin oxidoreductase, 4Fe-4S domain
897	1025	CDD	cd02792	MopB_CT_Formate-Dh-Na-like
510	687	Gene3D	G3DSA:3.40.50.740	-
3	1025	NCBIfam	TIGR01553	formate dehydrogenase-N subunit alpha
3	1025	InterPro	IPR006443	Formate dehydrogenase-N, alpha subunit
48	884	CDD	cd02752	MopB_Formate-Dh-Na-like
44	105	SMART	SM00926	Molybdop_Fe4S4_2
44	105	InterPro	IPR006963	Molybdopterin oxidoreductase, 4Fe-4S domain
36	160	FunFam	G3DSA:3.30.200.210:FF:000003	Formate dehydrogenase-N subunit alpha
1	10	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
837	1026	SUPERFAMILY	SSF50692	ADC-like
837	1026	InterPro	IPR009010	Aspartate decarboxylase-like domain superfamily
193	487	FunFam	G3DSA:3.40.228.10:FF:000006	Formate dehydrogenase, alpha subunit, selenocysteine-containing
193	491	Gene3D	G3DSA:3.40.228.10	Dimethylsulfoxide Reductase, domain 2
34	1026	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
765	847	Gene3D	G3DSA:3.40.228.10	Dimethylsulfoxide Reductase, domain 2
1	33	SignalP_GRAM_POSITIVE	SignalP-TM	SignalP-TM
848	1026	FunFam	G3DSA:2.40.40.20:FF:000017	Formate dehydrogenase, alpha subunit
37	160	Gene3D	G3DSA:3.30.200.210	-
1	33	ProSiteProfiles	PS51318	Twin arginine translocation (Tat) signal profile.
1	33	InterPro	IPR006311	Twin-arginine translocation pathway, signal sequence
1020	1026	Coils	Coil	Coil
1	33	Phobius	SIGNAL_PEPTIDE	Signal peptide region
11	24	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

Loading 3D structure...

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Structural evidence

0 + 1

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold PA4812	AlphaFold	—	—	full sequence	—	Viewing

Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
4				0.564
2				0.321

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.

60 records

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, 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
2MD	1H0H	Q934F5	742.6 Da LogP -2.53 TPSA 346.6	3 viol.	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@@](=…`
4MO	1AA6	P07658	95.9 Da LogP -0.00 TPSA 0.0	✓ Ro5	✓ Clean	`[Mo+4]`
6MO	6TG9	D5AQH0	95.9 Da LogP -0.00 TPSA 0.0	✓ Ro5	✓ Clean	`[Mo+6]`
CDL	1KQF	P24183	1464.1 Da LogP 23.31 TPSA 242.6	3 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](COP(=O)([O-])OCC(…`
FES	6TG9	D5AQH0	175.8 Da LogP 1.29 TPSA 0.0	✓ Ro5	✓ Clean	`S1[Fe]S[Fe]1`
H2S	6SDV	Q72EJ1	34.1 Da LogP 0.11 TPSA 0.0	✓ Ro5	✓ Clean	`S`
HQO	1KQG	P24183	259.3 Da LogP 3.69 TPSA 47.2	✓ Ro5	Alert	`CCCCCCCc1cc(c2ccccc2[n+]1[O-])O`
MGD	6SDV	Q72EJ1	740.6 Da LogP -2.06 TPSA 346.6	3 viol.	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@@](=…`
NO2	1FDI	P07658	46.0 Da LogP 0.25 TPSA 52.5	✓ Ro5	✓ Clean	`N(=O)[O-]`
W	6SDV	Q72EJ1	183.8 Da LogP -0.00 TPSA 0.0	✓ Ro5	✓ Clean	`[W+6]`

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
ZINC1529909	1.000	259.3 Da LogP 3.69 TPSA 47.2	✓ Ro5	Alert	`CCCCCCCc1cc(O)c2ccccc2[n+]1[O-]`
ZINC102191119	0.708	498.6 Da LogP 3.65 TPSA 148.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@@H](O)CO…`
ZINC58649551	0.708	498.6 Da LogP 3.65 TPSA 148.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@H](O)CO)…`
ZINC36178999	0.705	424.5 Da LogP 4.27 TPSA 119.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@@H](COP(=O)(O)O)OC(=O)CCCCCCC`
ZINC36179002	0.705	424.5 Da LogP 4.27 TPSA 119.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](COP(=O)(O)O)OC(=O)CCCCCCC`
ZINC104869865	0.684	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O…`
ZINC12504289	0.684	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC34541308	0.684	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC35000839	0.684	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC45284491	0.684	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC80639694	0.684	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC8215481	0.684	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC5820131	0.682	368.4 Da LogP 2.71 TPSA 119.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](COP(=O)(O)O)OC(=O)CCCCC`
ZINC5820134	0.682	368.4 Da LogP 2.71 TPSA 119.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](COP(=O)(O)O)OC(=O)CCCCC`
ZINC4521879	0.650	386.5 Da LogP 4.73 TPSA 78.9	✓ Ro5	✓ Clean	`CCCCCC(=O)OCC(COC(=O)CCCCC)OC(=O)CCCCC`
ZINC137999083	0.622	424.5 Da LogP 4.87 TPSA 113.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCCC(=O)OC[C@H](O)COP(=O)(O)O`
ZINC42851452	0.622	424.5 Da LogP 4.87 TPSA 113.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCCC(=O)OC[C@@H](O)COP(=O)(O)O`
ZINC62624856	0.622	382.4 Da LogP 3.70 TPSA 113.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@H](O)COP(=O)(O)O`
ZINC62624861	0.622	382.4 Da LogP 3.70 TPSA 113.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@@H](O)COP(=O)(O)O`
ZINC8218993	0.622	410.5 Da LogP 4.48 TPSA 113.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](O)COP(=O)(O)O`
ZINC8219000	0.622	410.5 Da LogP 4.48 TPSA 113.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@@H](O)COP(=O)(O)O`
ZINC102190506	0.620	467.5 Da LogP 4.25 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OCCN)OC(=O)CC…`
ZINC102190512	0.620	467.5 Da LogP 4.25 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)C…`
ZINC12501413	0.610	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)…`
ZINC12958448	0.610	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](COP(=O)(O)O)[C@H](O)[…`
ZINC1532555	0.610	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[…`
ZINC16546189	0.610	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](COP(=O)(O)O)[C@H](O)[…`
ZINC2159505	0.610	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)…`
ZINC3073318	0.610	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)…`
ZINC3869963	0.610	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)…`
ZINC3869965	0.610	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@@H](COP(=O)(O)O)[C@@H](O…`
ZINC9334496	0.610	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[…`
ZINC13552119	0.600	270.2 Da LogP 0.58 TPSA 113.3	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](O)COP(=O)(O)O`
ZINC27416437	0.600	411.4 Da LogP 2.69 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCCN)OC(=O)CCCCC`
ZINC33902364	0.600	411.4 Da LogP 2.69 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)CCC…`
ZINC36079847	0.591	344.5 Da LogP 4.15 TPSA 72.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@@H](CO)OC(=O)CCCCCCC`
ZINC8214428	0.591	344.5 Da LogP 4.15 TPSA 72.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO)OC(=O)CCCCCCC`
ZINC13543394	0.588	455.4 Da LogP 2.15 TPSA 171.7	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@H](N)C(=O)…`
ZINC4521911	0.585	344.4 Da LogP 3.56 TPSA 78.9	✓ Ro5	✓ Clean	`CCCCC(=O)OCC(COC(=O)CCCC)OC(=O)CCCC`
ZINC85603366	0.585	344.5 Da LogP 4.15 TPSA 72.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OCC(O)COC(=O)CCCCCCC`
ZINC13544781	0.585	482.6 Da LogP 4.22 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)OC[C@@H](CO[P@](=O)(O)OCC[N+](C)(C)C…`
ZINC13544783	0.585	482.6 Da LogP 4.22 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCC[N+](C)(C)C)…`
ZINC102191158	0.571	456.5 Da LogP 3.08 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@@](=O)(O)OC[C@…`
ZINC14880758	0.571	484.6 Da LogP 3.86 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@](=O)(O)OC[…`
ZINC14880760	0.571	484.6 Da LogP 3.86 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@](=O)(O)OC[C…`
ZINC53683910	0.571	484.6 Da LogP 3.86 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@@](=O)(O)OC[…`
ZINC62592202	0.571	456.5 Da LogP 3.08 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@@](=O)(O)OC[C@…`
ZINC62592203	0.571	456.5 Da LogP 3.08 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@@](=O)(O)OC[C…`
ZINC62592204	0.571	484.6 Da LogP 3.86 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@@](=O)(O)OC…`
ZINC96094841	0.571	456.5 Da LogP 3.08 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@@](=O)(O)OC[C…`

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.