Protein profile

PA0105

cytochrome C oxidase subunit II

Genome: NC_002516.2

Gene: PA0105 coxB Structure source: AlphaFold UniProt Q9I727

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Amino acids 374

Annotations 11

Features 51

PDB binders 28

Druggability 0.709

Overview

Basic information about this protein and its source genome.

Accession: PA0105
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA0105 coxB
Status: annotated
Amino acids: 374
Structure source: AlphaFold

7.1.1.9

GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. GO:0098803 Any protein complex that is part of a respiratory chain. GO:0005507 Binding to a copper (Cu) ion. GO:0004129 Catalysis of the reaction: 4 Fe(II)-[cytochrome c] + O2 + 8 H+(in) = 4 Fe(III)-[cytochrome c] + 2 H2O + 4 H+(out). GO:0020037 Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring. 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.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 37.278
Human E-value: 5.29e-38
Gut microbiome off-target: hit
Essential (DEG): N
Localization: CytoplasmicMembrane

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 0.709

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 10 GO

Enzyme Commission (EC)

7.1.1.9

Gene Ontology (GO)

GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
GO:0098803 Any protein complex that is part of a respiratory chain.
GO:0005507 Binding to a copper (Cu) ion.
GO:0004129 Catalysis of the reaction: 4 Fe(II)-[cytochrome c] + O2 + 8 H+(in) = 4 Fe(III)-[cytochrome c] + 2 H2O + 4 H+(out).
GO:0020037 Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring.
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:0042773 The transfer of electrons through a series of electron donors and acceptors, generating energy that is ultimately used for synthesis of ATP.
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:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
GO:0022900 A process in which a series of electron carriers operate together to transfer electrons from donors to any of several different terminal electron acceptors.

Sequence Features

Domain/signature hits from InterPro and related databases.

51 records

Show feature table

Start	End	DB	Term	Name
121	240	Pfam	PF00116	Cytochrome C oxidase subunit II, periplasmic domain
121	240	InterPro	IPR002429	Cytochrome c oxidase subunit II-like C-terminal
7	29	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
274	348	Pfam	PF13442	Cytochrome C oxidase, cbb3-type, subunit III
274	348	InterPro	IPR009056	Cytochrome c-like domain
224	241	PRINTS	PR01166	Cytochrome c oxidase subunit II signature
206	223	PRINTS	PR01166	Cytochrome c oxidase subunit II signature
186	206	PRINTS	PR01166	Cytochrome c oxidase subunit II signature
115	134	PRINTS	PR01166	Cytochrome c oxidase subunit II signature
81	93	PRINTS	PR01166	Cytochrome c oxidase subunit II signature
162	183	PRINTS	PR01166	Cytochrome c oxidase subunit II signature
93	113	PRINTS	PR01166	Cytochrome c oxidase subunit II signature
37	113	Gene3D	G3DSA:1.10.287.90	-
37	113	InterPro	IPR036257	Cytochrome C oxidase subunit II, transmembrane domain superfamily
187	235	ProSitePatterns	PS00078	CO II and nitrous oxide reductase dinuclear copper centers signature.
187	235	InterPro	IPR001505	Copper centre Cu(A)
1	22	SignalP_GRAM_POSITIVE	SignalP-TM	SignalP-TM
67	86	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
20	115	ProSiteProfiles	PS50999	Cytochrome oxidase subunit II transmembrane region profile.
20	115	InterPro	IPR011759	Cytochrome C oxidase subunit II, transmembrane domain
1	6	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
254	374	Gene3D	G3DSA:1.10.760.10	-
254	374	InterPro	IPR036909	Cytochrome c-like domain superfamily
46	66	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
87	105	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
87	109	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
273	353	ProSiteProfiles	PS51007	Cytochrome c family profile.
273	353	InterPro	IPR009056	Cytochrome c-like domain
37	113	FunFam	G3DSA:1.10.287.90:FF:000009	Cytochrome c oxidase subunit 2
44	66	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
1	22	Phobius	SIGNAL_PEPTIDE	Signal peptide region
12	112	SUPERFAMILY	SSF81464	Cytochrome c oxidase subunit II-like, transmembrane region
12	112	InterPro	IPR036257	Cytochrome C oxidase subunit II, transmembrane domain superfamily
114	252	Gene3D	G3DSA:2.60.40.420	-
114	252	InterPro	IPR008972	Cupredoxin
9	259	PANTHER	PTHR22888	CYTOCHROME C OXIDASE, SUBUNIT II
9	259	InterPro	IPR045187	Cytochrome c/quinol oxidase subunit II
23	104	Pfam	PF02790	Cytochrome C oxidase subunit II, transmembrane domain
23	104	InterPro	IPR011759	Cytochrome C oxidase subunit II, transmembrane domain
106	374	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
116	253	ProSiteProfiles	PS50857	Cytochrome oxidase subunit II copper A binding domain profile.
116	253	InterPro	IPR002429	Cytochrome c oxidase subunit II-like C-terminal
23	45	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
18	22	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
32	251	NCBIfam	TIGR02866	cytochrome c oxidase subunit II
32	251	InterPro	IPR014222	Cytochrome c oxidase, subunit II
116	257	SUPERFAMILY	SSF49503	Cupredoxins
116	257	InterPro	IPR008972	Cupredoxin
7	17	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
221	358	SUPERFAMILY	SSF46626	Cytochrome c
221	358	InterPro	IPR036909	Cytochrome c-like domain superfamily

3D Structure

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

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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 PA0105	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
2				0.709

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.

78 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
3PE	1M56	Q03736	748.1 Da LogP 12.06 TPSA 134.4	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](COP(=O)(O)OCCN)OC…`
4AG	2YEV	Q5SLI2	568.9 Da LogP 10.40 TPSA 72.8	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@@H](CO)OC(=O)CCCCCCCCC…`
5PL	2YEV	Q5SLI2	1233.7 Da LogP 15.13 TPSA 245.7	4 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCCCNC(=O)[C@@H](CO[C@@H]1[C@@H]…`
6PH	6GIQ	P00410	592.8 Da LogP 8.95 TPSA 119.4	2 viol.	✓ Clean	`CCCCCCCCCCCCCCC(=O)O[C@H](COC(=O)CCCCCCCCCCCC)C…`
7E8	2YEV	Q5SLI2	300.4 Da LogP 3.36 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCC/C=C\CCCCCC(=O)OC[C@@H](CO)O`
7E9	2YEV	Q5SLI2	300.4 Da LogP 3.36 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCC/C=C\CCCCCC(=O)OC(CO)CO`
7PH	6GIQ	P00410	564.7 Da LogP 8.17 TPSA 119.4	2 viol.	✓ Clean	`CCCCCCCCCCCCCC(=O)O[C@H](COC(=O)CCCCCCCCCCC)COP…`
8PE	6GIQ	P00410	692.0 Da LogP 10.50 TPSA 134.4	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OCC…`
9PE	6GIQ	P00410	593.8 Da LogP 7.77 TPSA 134.4	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)O[C@H](COC(=O)CCCCCC)CO[P…`
CDL	6HU9	P00410	1464.1 Da LogP 23.31 TPSA 242.6	3 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](COP(=O)([O-])OCC(…`
CN3	6GIQ	P00410	834.9 Da LogP 7.02 TPSA 236.9	3 viol.	✓ Clean	`CCCCCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@@H](C…`
CN5	6GIQ	P00410	634.6 Da LogP 5.59 TPSA 184.3	3 viol.	✓ Clean	`CCCCCCCCCCCCCCC(=O)OCCCO[P@](=O)(O)OC[C@H](CO[P…`
CUA	6GIQ	P00410	127.1 Da LogP -0.01 TPSA 0.0	✓ Ro5	✓ Clean	`[Cu][Cu]`
DMU	3OMN	Q3J5G0	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@H]1[C@@H]([C@H]([C@@H]([C@H](O1)C…`
DXC	3DTU	Q03736	392.6 Da LogP 4.48 TPSA 77.8	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)O)[C@H]1CC[C@@H]2[C@@]1([C@H](C[C…`
FES	6GIQ	P00410	175.8 Da LogP 1.29 TPSA 0.0	✓ Ro5	✓ Clean	`S1[Fe]S[Fe]1`
HTH	3OMN	Q3J5G0	148.2 Da LogP -0.11 TPSA 60.7	✓ Ro5	✓ Clean	`CCCC[C@H]([C@H](CO)O)O`
HTO	3DTU	Q03736	148.2 Da LogP -0.11 TPSA 60.7	✓ Ro5	✓ Clean	`CCCC[C@H]([C@@H](CO)O)O`
LDA	1AR1	P08306	229.4 Da LogP 4.48 TPSA 23.1	✓ Ro5	✓ Clean	`CCCCCCCCCCCC[N+](C)(C)[O-]`
LMT	3EHB	P08306	510.6 Da LogP -0.45 TPSA 178.5	3 viol.	✓ Clean	`CCCCCCCCCCCCO[C@H]1[C@@H]([C@H]([C@@H]([C@H](O1…`
LMU	5WEH	Q03736	510.6 Da LogP -0.45 TPSA 178.5	3 viol.	✓ Clean	`CCCCCCCCCCCCO[C@@H]1[C@@H]([C@H]([C@@H]([C@H](O…`
PCF	6HU9	P00410	734.1 Da LogP 10.61 TPSA 111.2	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](CO[P@](=O)([O-])OCC…`
PEF	6T0B	P00410	692.0 Da LogP 10.50 TPSA 134.4	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OCCN)…`
PEO	3HB3	P08306	34.0 Da LogP 0.02 TPSA 40.5	✓ Ro5	✓ Clean	`OO`
PER	3EHB	P08306	32.0 Da LogP -2.38 TPSA 46.1	✓ Ro5	✓ Clean	`[O-][O-]`
PTY	6YMX	P00410	734.1 Da LogP 11.67 TPSA 134.4	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCCCC(=O)O[C@H](COC(=O)CCCCCCCCC…`
TRD	3OMN	Q3J5G0	184.4 Da LogP 5.32 TPSA 0.0	1 viol.	✓ Clean	`CCCCCCCCCCCCC`
UQ6	6GIQ	P00410	592.9 Da LogP 11.56 TPSA 58.9	2 viol.	✓ Clean	`Cc1c(c(c(c(c1O)OC)OC)O)C\C=C(/C)\CC\C=C(/C)\CC\…`

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
ZINC100053689	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H]…`
ZINC100053691	1.000	496.6 Da LogP -0.84 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCCO[C@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC102190506	1.000	467.5 Da LogP 4.25 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OCCN)OC(=O)CC…`
ZINC12493596	1.000	392.6 Da LogP 4.48 TPSA 77.8	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)O)[C@H]1CC[C@H]2[C@@H]3CC[C@H]4C[…`
ZINC1501015302	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC1501016272	1.000	328.5 Da LogP 4.14 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCC/C=C\CCCCCCC(=O)OC[C@H](O)CO`
ZINC1501016273	1.000	328.5 Da LogP 4.14 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCC/C=C\CCCCCCC(=O)OC[C@@H](O)CO`
ZINC1501016315	1.000	314.5 Da LogP 3.75 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCC/C=C\CCCCCCC(=O)OC[C@@H](O)CO`
ZINC1501016316	1.000	314.5 Da LogP 3.75 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCC/C=C\CCCCCCC(=O)OC[C@H](O)CO`
ZINC2038077522	1.000	356.5 Da LogP 4.92 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCCC=CCCCCCCCC(=O)OC[C@@H](O)CO`
ZINC2038077523	1.000	356.5 Da LogP 4.92 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCCC=CCCCCCCCC(=O)OC[C@H](O)CO`
ZINC2039285653	1.000	454.5 Da LogP -2.01 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H](C…`
ZINC2039285654	1.000	454.5 Da LogP -2.01 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H](C…`
ZINC2053493146	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H]…`
ZINC2053493147	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H]…`
ZINC2053493149	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H]…`
ZINC221534416	1.000	328.5 Da LogP 4.14 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC/C=C\CCCCCC(=O)OC[C@@H](O)CO`
ZINC238809244	1.000	510.6 Da LogP -0.45 TPSA 178.5	3 viol.	✓ Clean	`CCCCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C…`
ZINC238809245	1.000	510.6 Da LogP -0.45 TPSA 178.5	3 viol.	✓ Clean	`CCCCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C…`
ZINC252695223	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC252695224	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC252695225	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC252695226	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC257356883	1.000	392.6 Da LogP 4.48 TPSA 77.8	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)O)[C@@H]1CC[C@@H]2[C@@H]3CC[C@H]4…`
ZINC257356885	1.000	392.6 Da LogP 4.48 TPSA 77.8	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)O)[C@@H]1CC[C@@H]2[C@@H]3CC[C@H]4…`
ZINC32840817	1.000	356.5 Da LogP 4.92 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC/C=C\CCCCCCCC(=O)OC(CO)CO`
ZINC32840818	1.000	356.5 Da LogP 4.92 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC/C=C/CCCCCCCC(=O)OC(CO)CO`
ZINC32840893	1.000	328.5 Da LogP 4.14 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCC/C=C\CCCCCCCC(=O)OC[C@@H](O)CO`
ZINC32840894	1.000	328.5 Da LogP 4.14 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCC/C=C/CCCCCCCC(=O)OC[C@@H](O)CO`
ZINC32840895	1.000	328.5 Da LogP 4.14 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCC/C=C\CCCCCCCC(=O)OC[C@H](O)CO`
ZINC32840896	1.000	328.5 Da LogP 4.14 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCC/C=C/CCCCCCCC(=O)OC[C@H](O)CO`
ZINC32840901	1.000	356.5 Da LogP 4.92 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC/C=C\CCCCCCCC(=O)OC[C@@H](O)CO`
ZINC32840902	1.000	356.5 Da LogP 4.92 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC/C=C/CCCCCCCC(=O)OC[C@@H](O)CO`
ZINC32840903	1.000	356.5 Da LogP 4.92 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC/C=C\CCCCCCCC(=O)OC[C@H](O)CO`
ZINC32840904	1.000	356.5 Da LogP 4.92 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC/C=C/CCCCCCCC(=O)OC[C@H](O)CO`
ZINC36079847	1.000	344.5 Da LogP 4.15 TPSA 72.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@@H](CO)OC(=O)CCCCCCC`
ZINC59978443	1.000	454.5 Da LogP -2.01 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H](…`
ZINC66157001	1.000	468.5 Da LogP -1.62 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H]…`
ZINC70669940	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O[C@H]2O[C@…`
ZINC70669941	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O[C@H]2O[C@…`
ZINC70669942	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O[C@H]2O[C@…`
ZINC70669943	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O[C@H]2O[C@…`
ZINC725433050	1.000	342.5 Da LogP 4.53 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC/C=C\CCCCCCC(=O)OC[C@@H](O)CO`
ZINC725433052	1.000	342.5 Da LogP 4.53 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC/C=C\CCCCCCC(=O)OC[C@H](O)CO`
ZINC77311968	1.000	454.5 Da LogP -2.01 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@@H]2O[C@H]…`
ZINC8214428	1.000	344.5 Da LogP 4.15 TPSA 72.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO)OC(=O)CCCCCCC`
ZINC83433913	1.000	426.5 Da LogP -2.79 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H](CO…`
ZINC85482724	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC86002923	1.000	426.5 Da LogP -2.79 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCO[C@@H]1O[C@H](CO)[C@H](O[C@H]2O[C@H](CO)…`
ZINC98208566	1.000	328.5 Da LogP 4.14 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC/C=C\CCCCCC(=O)OC[C@H](O)CO`

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.