Protein target profile

KP13_05503

Aspartate-semialdehyde dehydrogenase

Genome: KpKP13 Gene: AHE44509.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GTQ2

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Length 372

Pocket druggability 0.838

Direct ligand evidence 0 55 total records

Functional annotation 1 EC 12 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

Independent pocket support: FPocket + P2Rank Both predictors report a high-scoring binding site (FPocket 0.84, P2Rank 0.76). Use the 3D pocket comparison to verify whether they identify the same site. No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. Strong predicted binding pocket FPocket selected-pocket score 0.84. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.76. 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: 4.9% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 55.707 Higher values support similarity to known essential genes.
DEG E-value: 3.57e-153 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 97.26 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 0.838

Structure A0A0H3GTQ2

Pocket Pocket 1

P2Rank 0.76

Structure A0A0H3GTQ2

Pocket Pocket 1

ColabFold model

FPocket 0.418 · Pocket 4

P2Rank 0.681 · Pocket 1

Core conservation Accessory gene

Roary accessory

CoreCruncher accessory

Gut microbiome 234 / 4744 genomes with a hit

Prevalence 4.9%

Cross-references

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

Sequence

UniProt A0A0H3GTQ2

Chemistry

ChEMBL CHEMBL457665

Sequence

Primary amino-acid sequence viewer.

MKQVGIVGWRGMVGSVLLQRMIEENDFDDISAHFFSTSSAGAAGPVIKGKSDKLKDANSLSALAEMDIIITCQGGDYTKAIYPALTNSGWQGYWIDAASALRMDDNACIILDPVNRDNIDRAVKAGMKLFVGGNCSITLSLMGLAGLIKADLIEWMSVMTYQSASGAGAKQVREFIAQSAYISQHLSADELTASGSVLPLVNKVSELINSAGMPVENFGVPLMGSIIPWIDSDLGDGNSREEWKGEAETNKILGLASGTIPVNGLCIRVGVIRCHSAAITLKLKREVSEAEFAELVTHSHPWVNYIPNNKQESVSKLTPAAISGSLQVGIGRYKKMSLNNEPVYSVLTVGDQLLWGAAEPLRRMLNILLGKI

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 12 GO

Enzyme Commission (EC)

1.2.1.11

Gene Ontology (GO)

GO:0009089 OBSOLETE. The chemical reactions and pathways resulting in the formation of lysine, via the intermediate diaminopimelate.
GO:0009086 OBSOLETE. The chemical reactions and pathways resulting in the de novo formation of L-methionine (2-amino-4-(methylthio)butanoic acid), a sulfur-containing, essential amino acid found in peptide linkage in proteins.
GO:0009097 OBSOLETE. The chemical reactions and pathways resulting in the formation of isoleucine, (2R*,3R*)-2-amino-3-methylpentanoic acid.
GO:0009088 The chemical reactions and pathways resulting in the formation of L-threonine (2-amino-3-hydroxybutyric acid), a polar, uncharged, essential amino acid found in peptide linkage in proteins.
GO:0006520 The chemical reactions and pathways involving amino acids, carboxylic acids containing one or more amino groups.
GO:0004073 Catalysis of the reaction: L-aspartate 4-semialdehyde + NADP+ + phosphate = 4-phospho-L-aspartate + H+ + NADPH.
GO:0051287 Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH.
GO:0016620 Catalysis of an oxidation-reduction (redox) reaction in which an aldehyde or ketone (oxo) group acts as a hydrogen or electron donor and reduces NAD or NADP.
GO:0046983 The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits.
GO:0050661 Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH.
GO:0008652 The chemical reactions and pathways resulting in the formation of amino acids, organic acids containing one or more amino substituents.
GO:0019877 OBSOLETE. The chemical reactions and pathways resulting in the formation of diaminopimelate, both as an intermediate in lysine biosynthesis and as a component (as meso-diaminopimelate) of the peptidoglycan of Gram-negative bacterial cell walls.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

17 records

Show feature table

Start	End	DB	Term	Name
136	353	Gene3D	G3DSA:3.30.360.10	Dihydrodipicolinate Reductase; domain 2
2	369	NCBIfam	TIGR01745	aspartate-semialdehyde dehydrogenase
2	369	InterPro	IPR011534	Aspartate-semialdehyde dehydrogenase, gamma-type
1	147	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
1	147	InterPro	IPR036291	NAD(P)-binding domain superfamily
3	122	SMART	SM00859	Semialdhyde_dh_3
3	122	InterPro	IPR000534	Semialdehyde dehydrogenase, NAD-binding
144	355	Pfam	PF02774	Semialdehyde dehydrogenase, dimerisation domain
144	355	InterPro	IPR012280	Semialdehyde dehydrogenase, dimerisation domain
262	276	ProSitePatterns	PS01103	Aspartate-semialdehyde dehydrogenase signature.
262	276	InterPro	IPR000319	Aspartate-semialdehyde dehydrogenase, conserved site
134	356	SUPERFAMILY	SSF55347	Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain
1	372	PIRSF	PIRSF000148	ASA_dh
3	121	Pfam	PF01118	Semialdehyde dehydrogenase, NAD binding domain
3	121	InterPro	IPR000534	Semialdehyde dehydrogenase, NAD-binding
4	358	Gene3D	G3DSA:3.40.50.720	-
2	369	PANTHER	PTHR46278	DEHYDROGENASE, PUTATIVE-RELATED

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 · FPocket

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

Site 1 FPocket #1

0.838

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Surrounding area

Site 2 FPocket #18

0.599

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Surrounding area

Site 3 FPocket #8

0.244

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Surrounding area

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.76

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Surrounding area

Site 2 P2Rank #2

0.035

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Surrounding area

Site 3 P2Rank #3

0.025

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Surrounding area

Site 4 P2Rank #4

0.017

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Surrounding area

Site 5 P2Rank #5

0.009

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Surrounding area

Residue sets

UniProt: Active site:135-135 Acyl-thioester intermediate

UniProt: Active site:275-275 Proton acceptor

Binding pockets · FPocket

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

Site 1 FPocket #4

0.418

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Surrounding area

Site 2 FPocket #15

0.306

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Surrounding area

Site 3 FPocket #14

0.257

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Surrounding area

Site 4 FPocket #2

0.234

Likely same site as P2Rank 3 0.2 Å 10 shared residues 100% of smaller site

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Surrounding area

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.681

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Surrounding area

Site 2 P2Rank #2

0.064

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Surrounding area

Site 3 P2Rank #3

0.04

Likely same site as FPocket 2 0.2 Å 10 shared residues 100% of smaller site

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Surrounding area

Site 4 P2Rank #4

0.012

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Surrounding area

Site 5 P2Rank #5

0.005

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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_A0A0H3GTQ2	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_05503	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.

55 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 5 records from similar proteins

Structural ligands 4 0 loaded crystals

Measured bioactivity 1 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

4NO PDB via homolog 247.1 Da · LogP 0.10 · TPSA 138.0 Open detail RCSB PDB

CAC PDB via homolog Detail RCSB PDB

HSE PDB via homolog Detail RCSB PDB

PEJ PDB via homolog Detail RCSB PDB

CHEMBL457665 ChEMBL via homolog · pchembl 6.75 (~177.8 nM) 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.

Ligand	Source crystal	UniProt (homolog)	MW · LogP · TPSA	Lipinski	PAINS	SMILES
4NO RCSB PDB	4R5M	Q9KQG2	247.1 Da LogP 0.10 TPSA 138.0	✓ Ro5	✓ Clean	`c1cc(c(cc1[N+](=O)[O-])P(=O)(O)O)C(=O)O`
CAC RCSB PDB	1PQU	P44801	137.0 Da LogP -0.52 TPSA 40.1	✓ Ro5	✓ Clean	`C[As](=O)(C)[O-]`
HSE RCSB PDB	1PQP	P44801	119.1 Da LogP -1.22 TPSA 83.5	✓ Ro5	✓ Clean	`C(CO)[C@@H](C(=O)O)N`
PEJ RCSB PDB	1TB4	P44801	190.9 Da LogP -7.75 TPSA 92.2	✓ Ro5	✓ Clean	`[O-]I(=O)(=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).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
CHEMBL457665 ChEMBL	O25801	6.75 ~177.8 nM	201.2 Da LogP -1.07 TPSA 117.7	✓ Ro5	✓ Clean	`N[C@@H](CSS(=O)(=O)O)C(=O)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
ZINC1870296 ZINC	1.000	247.1 Da LogP 0.10 TPSA 138.0	✓ Ro5	✓ Clean	`O=C(O)c1ccc([N+](=O)[O-])cc1P(=O)(O)O`
ZINC1870301 ZINC	0.758	247.1 Da LogP 0.10 TPSA 138.0	✓ Ro5	✓ Clean	`O=C(O)c1cc([N+](=O)[O-])ccc1P(=O)(O)O`
ZINC157056 ZINC	0.656	211.1 Da LogP 0.99 TPSA 117.7	✓ Ro5	✓ Clean	`O=C(O)c1ccc([N+](=O)[O-])cc1C(=O)O`
ZINC1556249 ZINC	0.636	332.2 Da LogP 2.57 TPSA 160.9	✓ Ro5	✓ Clean	`O=C(O)c1ccc([N+](=O)[O-])cc1-c1cc([N+](=O)[O-])…`
ZINC1764711 ZINC	0.618	212.1 Da LogP 1.20 TPSA 123.6	✓ Ro5	✓ Clean	`O=C(O)c1ccc([N+](=O)[O-])cc1[N+](=O)[O-]`
ZINC1757911 ZINC	0.600	246.0 Da LogP 2.06 TPSA 80.4	✓ Ro5	✓ Clean	`O=C(O)c1ccc([N+](=O)[O-])cc1Br`
ZINC1870271 ZINC	0.600	282.0 Da LogP 1.16 TPSA 100.7	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(Br)c(P(=O)(O)O)c1`
ZINC1870306 ZINC	0.600	329.0 Da LogP 1.00 TPSA 100.7	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(I)c(P(=O)(O)O)c1`
ZINC199208276 ZINC	0.600	217.1 Da LogP 0.71 TPSA 100.7	✓ Ro5	✓ Clean	`Cc1ccc([N+](=O)[O-])cc1P(=O)(O)O`
ZINC32336 ZINC	0.600	201.6 Da LogP 1.95 TPSA 80.4	✓ Ro5	✓ Clean	`O=C(O)c1ccc([N+](=O)[O-])cc1Cl`
ZINC5427620 ZINC	0.600	293.0 Da LogP 1.90 TPSA 80.4	✓ Ro5	✓ Clean	`O=C(O)c1ccc([N+](=O)[O-])cc1I`
ZINC1717037 ZINC	0.588	332.2 Da LogP 2.57 TPSA 160.9	✓ Ro5	✓ Clean	`O=C(O)c1cc([N+](=O)[O-])ccc1-c1ccc([N+](=O)[O-]…`
ZINC1870299 ZINC	0.583	247.1 Da LogP 0.10 TPSA 138.0	✓ Ro5	✓ Clean	`O=C(O)c1cccc(P(=O)(O)O)c1[N+](=O)[O-]`
ZINC4290726 ZINC	0.583	225.2 Da LogP 0.92 TPSA 117.7	✓ Ro5	✓ Clean	`O=C(O)Cc1cc([N+](=O)[O-])ccc1C(=O)O`
ZINC156878 ZINC	0.571	201.6 Da LogP 1.95 TPSA 80.4	✓ Ro5	✓ Clean	`O=C(O)c1cc([N+](=O)[O-])ccc1Cl`
ZINC4404106 ZINC	0.571	212.1 Da LogP 1.20 TPSA 123.6	✓ Ro5	✓ Clean	`O=C(O)c1cc([N+](=O)[O-])ccc1[N+](=O)[O-]`
ZINC19801483 ZINC	0.568	223.2 Da LogP 2.59 TPSA 80.4	✓ Ro5	✓ Clean	`CC(C)(C)c1cc([N+](=O)[O-])ccc1C(=O)O`
ZINC2525761 ZINC	0.568	235.1 Da LogP 2.31 TPSA 80.4	✓ Ro5	✓ Clean	`O=C(O)c1ccc([N+](=O)[O-])cc1C(F)(F)F`
ZINC256243285 ZINC	0.568	311.0 Da LogP 1.24 TPSA 97.5	✓ Ro5	✓ Clean	`O=[IH2]c1cc([N+](=O)[O-])ccc1C(=O)O`
ZINC1870291 ZINC	0.556	217.1 Da LogP 0.71 TPSA 100.7	✓ Ro5	✓ Clean	`Cc1cc([N+](=O)[O-])ccc1P(=O)(O)O`
ZINC2559907 ZINC	0.556	293.0 Da LogP 1.90 TPSA 80.4	✓ Ro5	✓ Clean	`O=C(O)c1cc([N+](=O)[O-])ccc1I`
ZINC56845 ZINC	0.556	246.0 Da LogP 2.06 TPSA 80.4	✓ Ro5	✓ Clean	`O=C(O)c1cc([N+](=O)[O-])ccc1Br`
ZINC9592349 ZINC	0.556	287.2 Da LogP 2.66 TPSA 117.7	✓ Ro5	✓ Clean	`O=C(O)c1ccc(-c2ccc([N+](=O)[O-])cc2)cc1C(=O)O`
ZINC1587866 ZINC	0.553	247.2 Da LogP 0.54 TPSA 134.8	✓ Ro5	✓ Clean	`O=C(O)c1ccc([N+](=O)[O-])cc1S(=O)(=O)O`
ZINC1870298 ZINC	0.553	247.1 Da LogP 0.10 TPSA 138.0	✓ Ro5	✓ Clean	`O=C(O)c1ccc(P(=O)(O)O)cc1[N+](=O)[O-]`
ZINC39151303 ZINC	0.553	243.2 Da LogP 2.96 TPSA 80.4	✓ Ro5	✓ Clean	`O=C(O)c1ccc([N+](=O)[O-])cc1-c1ccccc1`
ZINC59910411 ZINC	0.552	217.2 Da LogP -1.13 TPSA 126.9	✓ Ro5	✓ Clean	`N[C@@H](CSOS(=O)(=O)O)C(=O)O`
ZINC19737412 ZINC	0.550	234.2 Da LogP 0.87 TPSA 111.2	✓ Ro5	✓ Clean	`O=C(O)c1ccc([N+](=O)[O-])cc1-n1cnnc1`
ZINC2924258 ZINC	0.550	494.4 Da LogP 3.40 TPSA 219.1	✓ Ro5	✓ Clean	`O=C(Nc1cc([N+](=O)[O-])ccc1C(=O)O)c1ccc(C(=O)Nc…`
ZINC5513707 ZINC	0.550	331.2 Da LogP 2.45 TPSA 152.7	✓ Ro5	✓ Clean	`O=C(O)c1cc([N+](=O)[O-])ccc1C(=O)Nc1ccc([N+](=O…`
ZINC165626269 ZINC	0.548	326.1 Da LogP -1.31 TPSA 189.7	1 viol.	✓ Clean	`O=C(O)c1cc(P(=O)(O)O)c(C(=O)O)cc1P(=O)(O)O`
ZINC2523035 ZINC	0.541	225.2 Da LogP 0.92 TPSA 117.7	✓ Ro5	✓ Clean	`O=C(O)Cc1ccc([N+](=O)[O-])cc1C(=O)O`
ZINC146578839 ZINC	0.538	246.2 Da LogP -0.06 TPSA 140.6	✓ Ro5	✓ Clean	`NS(=O)(=O)c1cc([N+](=O)[O-])ccc1C(=O)O`
ZINC1621825 ZINC	0.538	224.2 Da LogP 1.25 TPSA 109.5	✓ Ro5	✓ Clean	`CC(=O)Nc1cc([N+](=O)[O-])ccc1C(=O)O`
ZINC39426455 ZINC	0.538	225.2 Da LogP 1.08 TPSA 106.7	✓ Ro5	✓ Clean	`COC(=O)c1ccc([N+](=O)[O-])cc1C(=O)O`
ZINC4293805 ZINC	0.538	271.2 Da LogP 2.52 TPSA 97.5	✓ Ro5	✓ Clean	`O=C(O)c1ccc([N+](=O)[O-])cc1C(=O)c1ccccc1`
ZINC5131766 ZINC	0.538	224.3 Da LogP -1.26 TPSA 92.4	✓ Ro5	✓ Clean	`N[C@@H](CS)C(=O)N[C@@H](CS)C(=O)O`
ZINC2840030 ZINC	0.537	331.2 Da LogP 2.45 TPSA 152.7	✓ Ro5	✓ Clean	`O=C(Nc1cc([N+](=O)[O-])ccc1C(=O)O)c1ccc([N+](=O…`
ZINC285180 ZINC	0.537	286.2 Da LogP 2.55 TPSA 109.5	✓ Ro5	✓ Clean	`O=C(O)c1cc([N+](=O)[O-])ccc1C(=O)Nc1ccccc1`
ZINC9592202 ZINC	0.526	288.2 Da LogP 2.87 TPSA 123.6	✓ Ro5	✓ Clean	`O=C(O)c1cc([N+](=O)[O-])ccc1-c1ccc([N+](=O)[O-]…`
ZINC19869585 ZINC	0.525	255.3 Da LogP 3.18 TPSA 80.4	✓ Ro5	✓ Clean	`CC(C)(C)Sc1ccc([N+](=O)[O-])cc1C(=O)O`
ZINC2159899 ZINC	0.525	210.1 Da LogP 0.86 TPSA 109.5	✓ Ro5	✓ Clean	`O=CNc1cc([N+](=O)[O-])ccc1C(=O)O`
ZINC1730666 ZINC	0.524	208.2 Da LogP -1.46 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CSC[C@H](N)C(=O)O)C(=O)O`
ZINC1730667 ZINC	0.524	208.2 Da LogP -1.46 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CSC[C@H](N)C(=O)O)C(=O)O`
ZINC1730669 ZINC	0.524	208.2 Da LogP -1.46 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CSC[C@@H](N)C(=O)O)C(=O)O`
ZINC235386 ZINC	0.524	286.2 Da LogP 2.55 TPSA 109.5	✓ Ro5	✓ Clean	`O=C(Nc1cc([N+](=O)[O-])ccc1C(=O)O)c1ccccc1`
ZINC3055005 ZINC	0.524	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	0.524	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	0.524	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC68575534 ZINC	0.524	224.2 Da LogP 2.11 TPSA 92.5	✓ Ro5	✓ Clean	`CCCNc1cc([N+](=O)[O-])ccc1C(=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.