Protein profile

KP13_02396

Sulfite reductase [NADPH] flavoprotein alpha-component

Genome: KpKP13

Gene: cysJ AHE42967.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GWU1

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Amino acids 590

Annotations 9

Features 58

PDB binders 9

Druggability 0.412

Overview

Basic information about this protein and its source genome.

Accession: KP13_02396
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: cysJ AHE42967.1
Status: annotated
Amino acids: 590
Structure source: AlphaFold + ColabFold

1.8.1.2

GO:0004783 Catalysis of the reaction: hydrogen sulfide + 3 NADP+ + 3 H2O = sulfite + 3 NADPH + 3 H+. GO:0010181 Binding to flavin mono nucleotide. Flavin mono nucleotide (FMN) is the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes. GO:0019344 The chemical reactions and pathways resulting in the formation of L-cysteine, 2-amino-3-mercaptopropanoic acid. 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:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2. GO:0000103 The pathways by which inorganic sulfate is processed and incorporated into sulfated compounds.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 34.568
Human E-value: 1.3699999999999998e-60
Gut microbiome off-target: hit
Essential (DEG): N
DEG identity (%): 0.0
Localization: CytoplasmicMembrane
ColabFold pLDDT: 91.57

Selected Druggability evidence

AlphaFold / UniProt model

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 0.412

Structure A0A0H3GWU1

Pocket Pocket 18

P2Rank 0.614

Structure A0A0H3GWU1

Pocket Pocket 1

ColabFold model

FPocket 0.299 · Pocket 34

P2Rank 0.541 · Pocket 1

Core conservation Accessory gene

Roary core

CoreCruncher accessory

Gut microbiome 128 / 4744 genomes with a hit

Normalized 0.027

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Enzyme Commission (EC)

1.8.1.2

Gene Ontology (GO)

GO:0004783 Catalysis of the reaction: hydrogen sulfide + 3 NADP+ + 3 H2O = sulfite + 3 NADPH + 3 H+.
GO:0010181 Binding to flavin mono nucleotide. Flavin mono nucleotide (FMN) is the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
GO:0019344 The chemical reactions and pathways resulting in the formation of L-cysteine, 2-amino-3-mercaptopropanoic acid.
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:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.
GO:0000103 The pathways by which inorganic sulfate is processed and incorporated into sulfated compounds.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0070814 The chemical reactions and pathways resulting in the formation of hydrogen sulfide, H2S.

Sequence Features

Domain/signature hits from InterPro and related databases.

58 records

Show feature table

Start	End	DB	Term	Name
1	590	Hamap	MF_01541	Sulfite reductase [NADPH] flavoprotein alpha-component [cysJ].
1	590	InterPro	IPR029758	Sulphite reductase [NADPH] flavoprotein, alpha chain, Proteobacteria
271	375	Gene3D	G3DSA:1.20.990.10	-
271	375	InterPro	IPR023173	NADPH-cytochrome p450 reductase, FAD-binding, alpha-helical domain superfamily
51	585	PANTHER	PTHR19384	NITRIC OXIDE SYNTHASE-RELATED
45	210	FunFam	G3DSA:3.40.50.360:FF:000018	Sulfite reductase [NADPH] flavoprotein alpha-component
221	415	Pfam	PF00667	FAD binding domain
221	415	InterPro	IPR003097	Sulfite reductase [NADPH] flavoprotein alpha-component-like, FAD-binding
2	590	NCBIfam	TIGR01931	assimilatory sulfite reductase (NADPH) flavoprotein subunit
2	590	InterPro	IPR010199	Sulphite reductase [NADPH] flavoprotein, alpha chain
231	590	CDD	cd06199	SiR
54	200	SUPERFAMILY	SSF52218	Flavoproteins
54	200	InterPro	IPR029039	Flavoprotein-like superfamily
438	590	FunFam	G3DSA:3.40.50.80:FF:000001	NADPH--cytochrome P450 reductase 1
539	547	PRINTS	PR00371	Flavoprotein pyridine nucleotide cytochrome reductase signature
539	547	InterPro	IPR001709	Flavoprotein pyridine nucleotide cytochrome reductase
410	419	PRINTS	PR00371	Flavoprotein pyridine nucleotide cytochrome reductase signature
410	419	InterPro	IPR001709	Flavoprotein pyridine nucleotide cytochrome reductase
447	466	PRINTS	PR00371	Flavoprotein pyridine nucleotide cytochrome reductase signature
447	466	InterPro	IPR001709	Flavoprotein pyridine nucleotide cytochrome reductase
472	481	PRINTS	PR00371	Flavoprotein pyridine nucleotide cytochrome reductase signature
472	481	InterPro	IPR001709	Flavoprotein pyridine nucleotide cytochrome reductase
485	496	PRINTS	PR00371	Flavoprotein pyridine nucleotide cytochrome reductase signature
485	496	InterPro	IPR001709	Flavoprotein pyridine nucleotide cytochrome reductase
261	271	PRINTS	PR00371	Flavoprotein pyridine nucleotide cytochrome reductase signature
261	271	InterPro	IPR001709	Flavoprotein pyridine nucleotide cytochrome reductase
516	532	PRINTS	PR00371	Flavoprotein pyridine nucleotide cytochrome reductase signature
516	532	InterPro	IPR001709	Flavoprotein pyridine nucleotide cytochrome reductase
377	384	PRINTS	PR00371	Flavoprotein pyridine nucleotide cytochrome reductase signature
377	384	InterPro	IPR001709	Flavoprotein pyridine nucleotide cytochrome reductase
271	375	FunFam	G3DSA:1.20.990.10:FF:000004	Sulfite reductase [NADPH] flavoprotein alpha-component
58	186	Pfam	PF00258	Flavodoxin
58	186	InterPro	IPR008254	Flavodoxin/nitric oxide synthase
225	439	ProSiteProfiles	PS51384	Ferredoxin reductase-type FAD binding domain profile.
225	439	InterPro	IPR017927	FAD-binding domain, ferredoxin reductase-type
448	554	Pfam	PF00175	Oxidoreductase NAD-binding domain
448	554	InterPro	IPR001433	Oxidoreductase FAD/NAD(P)-binding
435	590	SUPERFAMILY	SSF52343	Ferredoxin reductase-like, C-terminal NADP-linked domain
435	590	InterPro	IPR039261	Ferredoxin-NADP reductase (FNR), nucleotide-binding domain
55	193	ProSiteProfiles	PS50902	Flavodoxin-like domain profile.
55	193	InterPro	IPR008254	Flavodoxin/nitric oxide synthase
44	210	Gene3D	G3DSA:3.40.50.360	-
44	210	InterPro	IPR029039	Flavoprotein-like superfamily
436	590	Gene3D	G3DSA:3.40.50.80	-
436	590	InterPro	IPR039261	Ferredoxin-NADP reductase (FNR), nucleotide-binding domain
1	590	PIRSF	PIRSF000207	SiR-FP_CysJ
1	590	InterPro	IPR010199	Sulphite reductase [NADPH] flavoprotein, alpha chain
218	437	SUPERFAMILY	SSF63380	Riboflavin synthase domain-like
218	437	InterPro	IPR017938	Riboflavin synthase-like beta-barrel
224	430	Gene3D	G3DSA:2.40.30.10	Translation factors
160	179	PRINTS	PR00369	Flavodoxin signature
160	179	InterPro	IPR001094	Flavodoxin-like
56	69	PRINTS	PR00369	Flavodoxin signature
56	69	InterPro	IPR001094	Flavodoxin-like
104	115	PRINTS	PR00369	Flavodoxin signature
104	115	InterPro	IPR001094	Flavodoxin-like
136	146	PRINTS	PR00369	Flavodoxin signature
136	146	InterPro	IPR001094	Flavodoxin-like

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 + 2

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

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold AF_A0A0H3GWU1	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_02396	ColabFold	—	—	full sequence	—	Loaded

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
18				0.412

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Score	Probability
1	5.24	0.244
2	2.93	0.094
3	2.88	0.091
4	2.15	0.05
5	2.02	0.044

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
34				0.299

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Score	Probability
1	3.79	0.147
2	3.1	0.104
3	2.44	0.066
4	2.33	0.06
5	1.93	0.04

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

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
2AM	4YAF	P00388	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
A2P	1FNC	P00455	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
CXS	6EFV	W8SX42	221.3 Da LogP 1.19 TPSA 66.4	✓ Ro5	✓ Clean	`C1CCC(CC1)NCCCS(=O)(=O)O`
EN6	6LI0	P00323	489.5 Da LogP 4.22 TPSA 87.4	✓ Ro5	✓ Clean	`Cc1c(c(n(n1)c2cccc3c2sc(c3)Cc4cccc(c4)C(F)(F)F)…`
FDA	5VW2	B4G043	787.6 Da LogP -1.75 TPSA 363.3	3 viol.	✓ Clean	`Cc1cc2c(cc1C)N(C3=C(N2)C(=O)NC(=O)N3)C[C@@H]([C…`
FLC	6LI0	P00323	189.1 Da LogP -5.25 TPSA 140.6	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O`
NCA	5VW4	B4G043	122.1 Da LogP 0.18 TPSA 56.0	✓ Ro5	✓ Clean	`c1cc(cnc1)C(=O)N`
OLC	6LI0	P00323	356.5 Da LogP 4.92 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC\C=C/CCCCCCCC(=O)OC[C@@H](CO)O`
RBF	1BU5	P00323	376.4 Da LogP -1.72 TPSA 161.6	✓ Ro5	✓ Clean	`Cc1cc2c(cc1C)N(C3=NC(=O)NC(=O)C3=N2)C[C@@H]([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
ZINC11565587	1.000	376.4 Da LogP -1.72 TPSA 161.6	✓ Ro5	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@@H](O)[C@H](O)…`
ZINC13424932	1.000	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@@H](O)[C@@H]1…`
ZINC13424933	1.000	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO)[C@@H](O)[C@@H]1O…`
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`
ZINC1532585	1.000	376.4 Da LogP -1.72 TPSA 161.6	✓ Ro5	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@@H](O)[C@@H](O…`
ZINC1769096	1.000	376.4 Da LogP -1.72 TPSA 161.6	✓ Ro5	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@H](O)[…`
ZINC2004372	1.000	221.3 Da LogP 1.19 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCCNC1CCCCC1`
ZINC2036187	1.000	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@H](O)[C@H]1OP…`
ZINC2036848	1.000	376.4 Da LogP -1.72 TPSA 161.6	✓ Ro5	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@H](O)[…`
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`
ZINC221534416	1.000	328.5 Da LogP 4.14 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC/C=C\CCCCCC(=O)OC[C@@H](O)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`
ZINC3650334	1.000	376.4 Da LogP -1.72 TPSA 161.6	✓ Ro5	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@@H](O)…`
ZINC3831422	1.000	376.4 Da LogP -1.72 TPSA 161.6	✓ Ro5	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@@H](O)[C@H](O)…`
ZINC3831423	1.000	376.4 Da LogP -1.72 TPSA 161.6	✓ Ro5	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@@H](O)…`
ZINC3831424	1.000	376.4 Da LogP -1.72 TPSA 161.6	✓ Ro5	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@@H](O)[C@@H](O…`
ZINC3861741	1.000	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@@H](O)[C@H]1O…`
ZINC44960119	1.000	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@H](O)[C@@H]1O…`
ZINC4513863	1.000	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](O)[C@@H]1…`
ZINC4513866	1.000	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@@H](O)[C@@H]…`
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`
ZINC98208566	1.000	328.5 Da LogP 4.14 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC/C=C\CCCCCC(=O)OC[C@H](O)CO`
ZINC4353342	0.957	406.4 Da LogP -2.36 TPSA 181.8	1 viol.	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@H](O)[…`
ZINC4353343	0.957	406.4 Da LogP -2.36 TPSA 181.8	1 viol.	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@@H](O)[C@H](O)…`
ZINC4353344	0.957	406.4 Da LogP -2.36 TPSA 181.8	1 viol.	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@@H](O)…`
ZINC4353345	0.957	406.4 Da LogP -2.36 TPSA 181.8	1 viol.	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@@H](O)[C@@H](O…`
ZINC32840885	0.943	300.4 Da LogP 3.36 TPSA 66.8	✓ Ro5	✓ Clean	`CCCC/C=C\CCCCCCCC(=O)OC[C@@H](O)CO`
ZINC38364153	0.926	235.3 Da LogP 1.58 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCCCNC1CCCCC1`
ZINC2053467566	0.919	354.5 Da LogP 4.70 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCC=CCC=CCCCCCCCC(=O)OC[C@@H](O)CO`
ZINC2053467567	0.919	354.5 Da LogP 4.70 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCC=CCC=CCCCCCCCC(=O)OC[C@H](O)CO`
ZINC29045599	0.919	354.5 Da LogP 4.70 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCC/C=C/C/C=C\CCCCCCCC(=O)OC[C@H](O)CO`
ZINC4557100	0.919	354.5 Da LogP 4.70 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCC/C=C\C/C=C\CCCCCCCC(=O)OC[C@H](O)CO`
ZINC4557101	0.919	354.5 Da LogP 4.70 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCC/C=C\C/C=C\CCCCCCCC(=O)OC[C@@H](O)CO`
ZINC5819989	0.919	354.5 Da LogP 4.70 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCC/C=C/C/C=C/CCCCCCCC(=O)OC[C@H](O)CO`
ZINC5819990	0.919	354.5 Da LogP 4.70 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCC/C=C/C/C=C/CCCCCCCC(=O)OC[C@@H](O)CO`
ZINC85425978	0.919	354.5 Da LogP 4.70 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCC/C=C\C/C=C/CCCCCCCC(=O)OC[C@H](O)CO`
ZINC29045446	0.892	352.5 Da LogP 4.47 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCC/C=C\C/C=C\C/C=C\CCCCC(=O)OC[C@@H](O)CO`
ZINC79090744	0.882	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@H](OP(=O)(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.