KpKP13 Protein target profile

S-ribosylhomocysteine lyase

Accession: KP13_16560

Gene: luxS ANJ86588.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A6A8ECI3

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Length 171

Pocket druggability (P2Rank · AlphaFold DB model) 0.166

Direct ligand evidence 0 57 total records

Functional annotation 1 EC 4 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

No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Moderate predicted binding pocket FPocket selected-pocket score 0.56. This supports review but is not experimental validation. 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: No hit
Gut microbiome similarity: 4.3% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 0.0 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 96.44 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

P2Rank's binding-site probability is the primary druggability signal shown across the app; FPocket's druggability score is shown alongside it for comparison. Both estimate small-molecule pocket quality after applying the curated structure priority — neither is experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

Druggability (P2Rank) 0.166

Structure A0A6A8ECI3

Pocket Pocket 1

Druggability (FPocket) 0.563

Structure A0A6A8ECI3

Pocket Pocket 1

ColabFold model

P2Rank 0.35 · Pocket 1

FPocket 0.359 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 205 / 4744 genomes with a hit

Prevalence 4.3%

Sequence

Primary amino-acid sequence viewer.

MPLLDSFTVDHTRMEAPAVRVAKKMNTPHGDEITVFDLRFCVPNQEVMPERGIHTLEHLFAGFMRDHLNGNGVEIIDISPMGCRTGFYMSLIGTPDEQRVADAWKAAMSDVLKVKDQNQIPELNVYQCGTYTMHSLEEAQDIARHIIERDVRINSNDELALPKEKLQELHI

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 4 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

4.4.1.21

Gene Ontology (GO)

GO:0043768 Catalysis of the reaction: S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = (S)-4,5-dihydroxypentane-2,3-dione + L-homocysteine.
GO:0005506 Binding to an iron (Fe) ion.
GO:0046872 Binding to a metal ion.
GO:0009372 The cell-cell signaling process in which single-celled organisms carry out coordinated responses by monitoring their own population density, and often also that of other microbes, by producing small, diffusible, signal molecules, detecting the concentration of these molecules, and triggering a signal transduction pathway when a certain threshold is reached. Quorum sensing can occur amongst microbial communities in the environment or within host organisms.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

22 records

Show feature table

Start	End	DB	Term	Name
1	159	PANTHER	PTHR35799	S-RIBOSYLHOMOCYSTEINE LYASE
1	159	InterPro	IPR003815	S-ribosylhomocysteinase (LuxS)
49	67	PRINTS	PR01487	Bacterial autoinducer-2 (AI-2) production protein LuxS signature
49	67	InterPro	IPR003815	S-ribosylhomocysteinase (LuxS)
28	46	PRINTS	PR01487	Bacterial autoinducer-2 (AI-2) production protein LuxS signature
28	46	InterPro	IPR003815	S-ribosylhomocysteinase (LuxS)
121	140	PRINTS	PR01487	Bacterial autoinducer-2 (AI-2) production protein LuxS signature
121	140	InterPro	IPR003815	S-ribosylhomocysteinase (LuxS)
5	23	PRINTS	PR01487	Bacterial autoinducer-2 (AI-2) production protein LuxS signature
5	23	InterPro	IPR003815	S-ribosylhomocysteinase (LuxS)
77	95	PRINTS	PR01487	Bacterial autoinducer-2 (AI-2) production protein LuxS signature
77	95	InterPro	IPR003815	S-ribosylhomocysteinase (LuxS)
1	171	Gene3D	G3DSA:3.30.1360.80	-
1	171	InterPro	IPR037005	S-ribosylhomocysteinase (LuxS) superfamily
1	162	PIRSF	PIRSF006160	AI2
1	162	InterPro	IPR003815	S-ribosylhomocysteinase (LuxS)
4	152	Pfam	PF02664	S-Ribosylhomocysteinase (LuxS)
4	152	InterPro	IPR003815	S-ribosylhomocysteinase (LuxS)
1	159	Hamap	MF_00091	S-ribosylhomocysteine lyase [luxS].
1	171	FunFam	G3DSA:3.30.1360.80:FF:000001	S-ribosylhomocysteine lyase
4	162	SUPERFAMILY	SSF63411	LuxS/MPP-like metallohydrolase
4	162	InterPro	IPR011249	Metalloenzyme, LuxS/M16 peptidase-like

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 · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.166

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Surrounding area

Pocket 2 P2Rank #2

0.069

Likely same site as FPocket 1 1.3 Å 9 shared residues 100% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.065

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Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #1

0.563

Likely same site as P2Rank 2 1.3 Å 9 shared residues 100% of smaller site

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Surrounding area

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.35

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Surrounding area

Pocket 2 P2Rank #2

0.083

Likely same site as FPocket 3 2.0 Å 9 shared residues 100% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.027

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Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #1

0.359

Show in viewer

Surrounding area

Pocket 2 FPocket #3

0.237

Likely same site as P2Rank 2 2.0 Å 9 shared residues 100% of smaller site

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_A0A6A8ECI3	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_16560	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.

57 records

Chemistry signal

Bioactivity evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 7 records from similar proteins

Structural ligands 0 0 loaded crystals

Measured bioactivity 7 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

CHEMBL208091 ChEMBL via homolog pchembl 6.43 (~371.5 nM) 268.3 Da · LogP -2.25 · TPSA 153.1 Open detail ChEMBL

CHEMBL593446 ChEMBL via homolog · pchembl 6.37 (~426.6 nM) Detail ChEMBL

CHEMBL595659 ChEMBL via homolog · pchembl 6.16 (~691.8 nM) Detail ChEMBL

CHEMBL207406 ChEMBL via homolog · pchembl 6.14 (~724.4 nM) Detail ChEMBL

CHEMBL1078480 ChEMBL via homolog Detail ChEMBL

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.

No PDB ligands found through similar proteins.

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
CHEMBL208091 ChEMBL	O34667	6.43 ~371.5 nM	268.3 Da LogP -2.25 TPSA 153.1	1 viol.	✓ Clean	`N[C@@H](CCSC[C@H](O)[C@@H](O)C(=O)NO)C(=O)O`
CHEMBL593446 ChEMBL	O34667	6.37 ~426.6 nM	267.3 Da LogP -2.04 TPSA 133.2	✓ Ro5	✓ Clean	`N[C@@H](CCSC[C@H]1OC(O)[C@H](O)[C@@H]1O)C(=O)O`
CHEMBL595659 ChEMBL	O34667	6.16 ~691.8 nM	269.3 Da LogP -1.06 TPSA 113.0	✓ Ro5	✓ Clean	`N[C@@H](CCSC[C@H]1OC(O)[C@H](O)[C@@H]1F)C(=O)O`
CHEMBL207406 ChEMBL	O34667	6.14 ~724.4 nM	268.3 Da LogP -2.25 TPSA 153.1	1 viol.	✓ Clean	`N[C@@H](CCSC[C@@H](O)[C@@H](O)C(=O)NO)C(=O)O`
CHEMBL1078480 ChEMBL	P45578	—	310.0 Da LogP 3.62 TPSA 26.3	✓ Ro5	✓ Clean	`CCCCC1=CC(=C(Br)Br)OC1=O`
CHEMBL1078481 ChEMBL	P45578	—	253.9 Da LogP 2.06 TPSA 26.3	✓ Ro5	✓ Clean	`O=C1C=CC(=C(Br)Br)O1`
CHEMBL448241 ChEMBL	P45578	—	310.0 Da LogP 3.62 TPSA 26.3	✓ Ro5	✓ Clean	`CCCCC1=C(Br)/C(=C/Br)OC1=O`

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
ZINC1762530 ZINC	1.000	253.9 Da LogP 2.06 TPSA 26.3	✓ Ro5	✓ Clean	`O=C1C=CC(=C(Br)Br)O1`
ZINC1674993 ZINC	0.640	296.4 Da LogP 0.06 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCSCCSCC[C@H](N)C(=O)O)C(=O)O`
ZINC1674994 ZINC	0.640	296.4 Da LogP 0.06 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCSCCSCC[C@@H](N)C(=O)O)C(=O)O`
ZINC1674996 ZINC	0.640	296.4 Da LogP 0.06 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCSCCSCC[C@@H](N)C(=O)O)C(=O)O`
ZINC1529407 ZINC	0.615	222.3 Da LogP -1.07 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCSC[C@@H](N)C(=O)O)C(=O)O`
ZINC1532680 ZINC	0.615	222.3 Da LogP -1.07 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCSC[C@H](N)C(=O)O)C(=O)O`
ZINC1708208 ZINC	0.615	222.3 Da LogP -1.07 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CSCC[C@@H](N)C(=O)O)C(=O)O`
ZINC1605257 ZINC	0.613	280.4 Da LogP 0.39 TPSA 92.4	✓ Ro5	✓ Clean	`CSCC[C@H](N)C(=O)N[C@@H](CCSC)C(=O)O`
ZINC1605258 ZINC	0.613	280.4 Da LogP 0.39 TPSA 92.4	✓ Ro5	✓ Clean	`CSCC[C@H](NC(=O)[C@H](N)CCSC)C(=O)O`
ZINC1605259 ZINC	0.613	280.4 Da LogP 0.39 TPSA 92.4	✓ Ro5	✓ Clean	`CSCC[C@H](N)C(=O)N[C@H](CCSC)C(=O)O`
ZINC1605260 ZINC	0.613	280.4 Da LogP 0.39 TPSA 92.4	✓ Ro5	✓ Clean	`CSCC[C@@H](N)C(=O)N[C@H](CCSC)C(=O)O`
ZINC2384801 ZINC	0.613	220.3 Da LogP -0.34 TPSA 92.4	✓ Ro5	✓ Clean	`CSCC[C@H](N)C(=O)N[C@@H](C)C(=O)O`
ZINC4556875 ZINC	0.613	220.3 Da LogP -0.34 TPSA 92.4	✓ Ro5	✓ Clean	`CSCC[C@@H](N)C(=O)N[C@@H](C)C(=O)O`
ZINC4556876 ZINC	0.613	220.3 Da LogP -0.34 TPSA 92.4	✓ Ro5	✓ Clean	`CSCC[C@@H](N)C(=O)N[C@H](C)C(=O)O`
ZINC4556877 ZINC	0.613	220.3 Da LogP -0.34 TPSA 92.4	✓ Ro5	✓ Clean	`CSCC[C@H](N)C(=O)N[C@H](C)C(=O)O`
ZINC1708207 ZINC	0.606	222.3 Da LogP -1.07 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCSC[C@H](N)C(=O)O)C(=O)O`
ZINC1569523 ZINC	0.581	206.3 Da LogP -0.73 TPSA 92.4	✓ Ro5	✓ Clean	`CSCC[C@@H](N)C(=O)NCC(=O)O`
ZINC1593212 ZINC	0.581	206.3 Da LogP -0.73 TPSA 92.4	✓ Ro5	✓ Clean	`CSCC[C@H](N)C(=O)NCC(=O)O`
ZINC2384813 ZINC	0.576	236.3 Da LogP -1.37 TPSA 112.7	✓ Ro5	✓ Clean	`CSCC[C@H](N)C(=O)N[C@@H](CO)C(=O)O`
ZINC2384835 ZINC	0.576	264.3 Da LogP -0.89 TPSA 129.7	✓ Ro5	✓ Clean	`CSCC[C@H](N)C(=O)N[C@@H](CC(=O)O)C(=O)O`
ZINC2390943 ZINC	0.576	248.3 Da LogP 0.29 TPSA 92.4	✓ Ro5	✓ Clean	`CSCC[C@H](N)C(=O)N[C@H](C(=O)O)C(C)C`
ZINC4557150 ZINC	0.576	236.3 Da LogP -1.37 TPSA 112.7	✓ Ro5	✓ Clean	`CSCC[C@H](N)C(=O)N[C@H](CO)C(=O)O`
ZINC4899465 ZINC	0.576	411.6 Da LogP 0.63 TPSA 121.5	✓ Ro5	✓ Clean	`CSCC[C@H](N)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCSC…`
ZINC64219373 ZINC	0.576	411.6 Da LogP 0.63 TPSA 121.5	✓ Ro5	✓ Clean	`CSCC[C@H](N)C(=O)N[C@@H](CCSC)C(=O)N[C@H](CCSC)…`
ZINC11755051 ZINC	0.567	204.3 Da LogP 0.94 TPSA 46.3	✓ Ro5	✓ Clean	`CCN(CC)C(=O)[C@@H](N)CCSC`
ZINC57358674 ZINC	0.567	205.3 Da LogP 1.41 TPSA 52.3	✓ Ro5	✓ Clean	`CSCC[C@H](N)C(=O)OC(C)(C)C`
ZINC57933694 ZINC	0.567	205.3 Da LogP 1.41 TPSA 52.3	✓ Ro5	✓ Clean	`CSCC[C@@H](N)C(=O)OC(C)(C)C`
ZINC62725402 ZINC	0.567	204.3 Da LogP 0.94 TPSA 46.3	✓ Ro5	✓ Clean	`CCN(CC)C(=O)[C@H](N)CCSC`
ZINC2522690 ZINC	0.563	220.3 Da LogP -0.34 TPSA 92.4	✓ Ro5	✓ Clean	`CSCC[C@H](N)C(=O)NCCC(=O)O`
ZINC1698833 ZINC	0.552	203.2 Da LogP 1.04 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](CCSC(F)(F)F)C(=O)O`
ZINC2041757 ZINC	0.552	203.2 Da LogP 1.04 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](CCSC(F)(F)F)C(=O)O`
ZINC1576323 ZINC	0.543	263.3 Da LogP -1.49 TPSA 135.5	✓ Ro5	✓ Clean	`CSCC[C@H](N)C(=O)N[C@@H](CC(N)=O)C(=O)O`
ZINC1576325 ZINC	0.543	263.3 Da LogP -1.49 TPSA 135.5	✓ Ro5	✓ Clean	`CSCC[C@H](N)C(=O)N[C@H](CC(N)=O)C(=O)O`
ZINC2390945 ZINC	0.543	262.4 Da LogP 0.68 TPSA 92.4	✓ Ro5	✓ Clean	`CSCC[C@H](N)C(=O)N[C@@H](CC(C)C)C(=O)O`
ZINC2516118 ZINC	0.543	278.3 Da LogP -0.50 TPSA 129.7	✓ Ro5	✓ Clean	`CSCC[C@H](N)C(=O)N[C@@H](CCC(=O)O)C(=O)O`
ZINC4557160 ZINC	0.543	262.4 Da LogP 0.68 TPSA 92.4	✓ Ro5	✓ Clean	`CSCC[C@@H](N)C(=O)N[C@@H](CC(C)C)C(=O)O`
ZINC4557161 ZINC	0.543	262.4 Da LogP 0.68 TPSA 92.4	✓ Ro5	✓ Clean	`CSCC[C@@H](N)C(=O)N[C@H](CC(C)C)C(=O)O`
ZINC4557162 ZINC	0.543	262.4 Da LogP 0.68 TPSA 92.4	✓ Ro5	✓ Clean	`CSCC[C@H](N)C(=O)N[C@H](CC(C)C)C(=O)O`
ZINC3055005 ZINC	0.542	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCC[C@H](N)C(=O)O)C(=O)O`
ZINC3055007 ZINC	0.542	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC3055010 ZINC	0.542	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC106506744 ZINC	0.531	303.5 Da LogP 4.44 TPSA 63.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCSCC[C@H](N)C(=O)O`
ZINC11754909 ZINC	0.531	204.3 Da LogP 0.84 TPSA 55.1	✓ Ro5	✓ Clean	`CSCC[C@H](N)C(=O)NCC(C)C`
ZINC11754910 ZINC	0.531	202.3 Da LogP 0.69 TPSA 46.3	✓ Ro5	✓ Clean	`CSCC[C@H](N)C(=O)N1CCCC1`
ZINC1757778 ZINC	0.531	222.3 Da LogP 0.37 TPSA 66.6	✓ Ro5	✓ Clean	`CN(C)C(=S)SCC[C@H](N)C(=O)O`
ZINC2033572 ZINC	0.531	222.3 Da LogP 0.37 TPSA 66.6	✓ Ro5	✓ Clean	`CN(C)C(=S)SCC[C@@H](N)C(=O)O`
ZINC34175843 ZINC	0.531	202.3 Da LogP 0.69 TPSA 46.3	✓ Ro5	✓ Clean	`CSCC[C@@H](N)C(=O)N1CCCC1`
ZINC62725431 ZINC	0.531	204.3 Da LogP 0.84 TPSA 55.1	✓ Ro5	✓ Clean	`CSCC[C@@H](N)C(=O)NCC(C)C`
ZINC62725433 ZINC	0.531	204.3 Da LogP 0.98 TPSA 55.1	✓ Ro5	✓ Clean	`CC[C@@H](C)NC(=O)[C@H](N)CCSC`
ZINC62725435 ZINC	0.531	204.3 Da LogP 0.98 TPSA 55.1	✓ Ro5	✓ Clean	`CC[C@H](C)NC(=O)[C@H](N)CCSC`

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.

Cross-references

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

Sequence

UniProt A0A6A8ECI3

Chemistry

ChEMBL CHEMBL208091 ChEMBL CHEMBL593446 ChEMBL CHEMBL595659 ChEMBL CHEMBL207406 ChEMBL CHEMBL1078480 ChEMBL CHEMBL1078481 ChEMBL CHEMBL448241