Protein target profile

KP13_03831

Succinyl-diaminopimelate desuccinylase

Genome: KpKP13 Gene: AHE43315.1 dapE 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3H1C2

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Length 375

Pocket druggability 0.44

Direct ligand evidence 0 54 total records

Functional annotation 1 EC 8 GO

Target summary

Target candidate with partial support; inspect missing evidence before prioritizing.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Main supporting evidence

Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Moderate predicted binding pocket FPocket selected-pocket score 0.44. This supports review but is not experimental validation. Structure available AlphaFold DB model + ColabFold model Ligand evidence via structure/bioactivity 4 structural and 0 bioactivity records.

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: Hit
Human identity (%): 42.857 Lower values reduce human off-target concern.
Human E-value: 2.76e-07
Gut microbiome similarity: 4.2% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 92.0 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Unknown

Structure confidence

ColabFold pLDDT: 97.08 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 0.44

Structure A0A0H3H1C2

Pocket Pocket 3

P2Rank 0.476

Structure A0A0H3H1C2

Pocket Pocket 1

ColabFold model

FPocket 0.442 · Pocket 1

P2Rank 0.458 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 200 / 4744 genomes with a hit

Prevalence 4.2%

Cross-references

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

Sequence

UniProt A0A0H3H1C2

Sequence

Primary amino-acid sequence viewer.

MSCPVIELAQQLIRRPSLSPDDAGCQALMIERLRAIGFTVEPMDFGDTQNFWAWRGHGETLAFAGHTDVVPAGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVATERFVAQYPNHRGRLAFLITSDEEASAKNGTVKVVETLMARNERLDYCLVGEPSSTEVVGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAELVNIEWDKGNEFFPPTSMQIANVQSGTGSNNVIPGDMFVQFNFRFSTELTDEMIKSRVIALLEKYQLRYSVEWWLSGQPFLTGRGKLVDAVVNAIEHYNEIKPQLLTNGGTSDGRFIARMGAQVVELGPVNATIHKINECVNAADLQLLARMYQRVMEQLVA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Enzyme Commission (EC)

3.5.1.18

Gene Ontology (GO)

GO:0009014 Catalysis of the reaction: N-succinyl-LL-2,6-diaminopimelate + H2O = LL-2,6-diaminopimelate + succinate.
GO:0009089 OBSOLETE. The chemical reactions and pathways resulting in the formation of lysine, via the intermediate diaminopimelate.
GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.
GO:0008777 Catalysis of the reaction: N2-acetyl-L-ornithine + H2O = acetate + L-ornithine.
GO:0050897 Binding to a cobalt ion (Co2+).
GO:0008270 Binding to a zinc ion (Zn).
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.
GO:0006526 The chemical reactions and pathways resulting in the formation of arginine, 2-amino-5-(carbamimidamido)pentanoic acid.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

22 records

Show feature table

Start	End	DB	Term	Name
256	375	Gene3D	G3DSA:3.40.630.10	Zn peptidases
61	70	ProSitePatterns	PS00758	ArgE / dapE / ACY1 / CPG2 / yscS family signature 1.
61	70	InterPro	IPR001261	ArgE/DapE/ACY1/CPG2/YscS, conserved site
179	289	FunFam	G3DSA:3.30.70.360:FF:000011	Succinyl-diaminopimelate desuccinylase
255	375	FunFam	G3DSA:3.40.630.10:FF:000010	Succinyl-diaminopimelate desuccinylase
3	244	Gene3D	G3DSA:3.40.630.10	Zn peptidases
6	373	NCBIfam	TIGR01246	succinyl-diaminopimelate desuccinylase
6	373	InterPro	IPR005941	Succinyl-diaminopimelate desuccinylase, proteobacteria
3	244	FunFam	G3DSA:3.40.630.10:FF:000005	Succinyl-diaminopimelate desuccinylase
5	373	PANTHER	PTHR43808	ACETYLORNITHINE DEACETYLASE
97	136	ProSitePatterns	PS00759	ArgE / dapE / ACY1 / CPG2 / yscS family signature 2.
97	136	InterPro	IPR001261	ArgE/DapE/ACY1/CPG2/YscS, conserved site
62	371	Pfam	PF01546	Peptidase family M20/M25/M40
62	371	InterPro	IPR002933	Peptidase M20
175	280	Pfam	PF07687	Peptidase dimerisation domain
175	280	InterPro	IPR011650	Peptidase M20, dimerisation domain
6	370	CDD	cd03891	M20_DapE_proteobac
3	375	Hamap	MF_01690	Succinyl-diaminopimelate desuccinylase [dapE].
3	375	InterPro	IPR005941	Succinyl-diaminopimelate desuccinylase, proteobacteria
179	287	SUPERFAMILY	SSF55031	Bacterial exopeptidase dimerisation domain
179	287	InterPro	IPR036264	Bacterial exopeptidase dimerisation domain
5	373	SUPERFAMILY	SSF53187	Zn-dependent exopeptidases

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 #3

0.44

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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

0.476

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Surrounding area

Site 2 P2Rank #2

0.005

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Surrounding area

Site 3 P2Rank #3

0.001

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Surrounding area

Residue sets

UniProt: Active site:133-133 Proton acceptor

UniProt: Active site:68-68

UniProt: Binding site:134-134

UniProt: Binding site:162-162

UniProt: Binding site:348-348

UniProt: Binding site:66-66

UniProt: Binding site:99-99

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.458

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Surrounding area

Site 2 P2Rank #2

0.019

Likely same site as FPocket 1 6.2 Å 5 shared residues 56% of smaller site

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Surrounding area

Site 3 P2Rank #3

0.009

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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_A0A0H3H1C2	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_03831	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.

54 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 4 records from similar proteins

Structural ligands 4 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

API PDB via homolog 190.2 Da · LogP -1.02 · TPSA 126.6 Open detail RCSB PDB

BES PDB via homolog Detail RCSB PDB

SIN PDB via homolog Detail RCSB PDB

X8Z PDB via homolog Detail RCSB PDB

ZINC11592554 ZINC proposed compound · Tanimoto 1.000 Detail ZINC

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
API RCSB PDB	5VO3	P44514	190.2 Da LogP -1.02 TPSA 126.6	✓ Ro5	✓ Clean	`C(C[C@H](C(=O)O)N)C[C@@H](C(=O)O)N`
BES RCSB PDB	4RUH	Q96KP4	308.4 Da LogP 0.53 TPSA 112.7	✓ Ro5	✓ Clean	`CC(C)C[C@@H](C(=O)O)NC(=O)[C@H]([C@@H](Cc1ccccc…`
SIN RCSB PDB	5VO3	P44514	118.1 Da LogP -0.06 TPSA 74.6	✓ Ro5	✓ Clean	`C(CC(=O)O)C(=O)O`
X8Z RCSB PDB	4PQA	Q9JYL2	217.3 Da LogP 0.63 TPSA 57.6	✓ Ro5	✓ Clean	`C[C@H](CS)C(=O)N1CCC[C@H]1C(=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).

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
ZINC11592554 ZINC	1.000	308.4 Da LogP 0.53 TPSA 112.6	✓ Ro5	✓ Clean	`CC(C)C[C@@H](NC(=O)[C@@H](O)[C@@H](N)Cc1ccccc1)…`
ZINC11592555 ZINC	1.000	308.4 Da LogP 0.53 TPSA 112.6	✓ Ro5	✓ Clean	`CC(C)C[C@@H](NC(=O)[C@H](O)[C@@H](N)Cc1ccccc1)C…`
ZINC11592556 ZINC	1.000	308.4 Da LogP 0.53 TPSA 112.6	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)[C@H](O)[C@@H](N)Cc1ccccc1)C(…`
ZINC1532730 ZINC	1.000	308.4 Da LogP 0.53 TPSA 112.6	✓ Ro5	✓ Clean	`CC(C)C[C@@H](NC(=O)[C@@H](O)[C@H](N)Cc1ccccc1)C…`
ZINC1542895 ZINC	1.000	308.4 Da LogP 0.53 TPSA 112.6	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)[C@@H](O)[C@H](N)Cc1ccccc1)C(…`
ZINC1558987 ZINC	1.000	308.4 Da LogP 0.53 TPSA 112.6	✓ Ro5	✓ Clean	`CC(C)C[C@@H](NC(=O)[C@H](O)[C@H](N)Cc1ccccc1)C(…`
ZINC20226 ZINC	1.000	217.3 Da LogP 0.63 TPSA 57.6	✓ Ro5	✓ Clean	`C[C@H](CS)C(=O)N1CCC[C@@H]1C(=O)O`
ZINC2545165 ZINC	1.000	308.4 Da LogP 0.53 TPSA 112.6	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)[C@H](O)[C@H](N)Cc1ccccc1)C(=…`
ZINC57000 ZINC	1.000	217.3 Da LogP 0.63 TPSA 57.6	✓ Ro5	✓ Clean	`C[C@@H](CS)C(=O)N1CCC[C@H]1C(=O)O`
ZINC57001 ZINC	1.000	217.3 Da LogP 0.63 TPSA 57.6	✓ Ro5	✓ Clean	`C[C@H](CS)C(=O)N1CCC[C@H]1C(=O)O`
ZINC57002 ZINC	1.000	217.3 Da LogP 0.63 TPSA 57.6	✓ Ro5	✓ Clean	`C[C@@H](CS)C(=O)N1CCC[C@@H]1C(=O)O`
ZINC7996813 ZINC	1.000	308.4 Da LogP 0.53 TPSA 112.6	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)[C@@H](O)[C@@H](N)Cc1ccccc1)C…`
ZINC3055005 ZINC	0.882	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	0.882	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	0.882	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC1555366 ZINC	0.833	232.3 Da LogP 0.15 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCCC[C@H](N)C(=O)O)C(=O)O`
ZINC1555367 ZINC	0.833	232.3 Da LogP 0.15 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC1555369 ZINC	0.833	232.3 Da LogP 0.15 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC1720127 ZINC	0.833	218.3 Da LogP -0.24 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCC[C@H](N)C(=O)O)C(=O)O`
ZINC1720128 ZINC	0.833	218.3 Da LogP -0.24 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC1720130 ZINC	0.833	218.3 Da LogP -0.24 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC95572961 ZINC	0.829	321.4 Da LogP 0.19 TPSA 104.5	✓ Ro5	✓ Clean	`CNC(=O)[C@H](CC(C)C)NC(=O)[C@@H](O)[C@H](N)Cc1c…`
ZINC1573805 ZINC	0.810	324.4 Da LogP 0.24 TPSA 132.9	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)[C@@H](O)[C@H](N)Cc1ccc(O)cc1…`
ZINC17125728 ZINC	0.810	324.4 Da LogP 0.24 TPSA 132.9	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)[C@@H](O)[C@@H](N)Cc1ccc(O)cc…`
ZINC17125733 ZINC	0.810	324.4 Da LogP 0.24 TPSA 132.9	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)[C@H](O)[C@@H](N)Cc1ccc(O)cc1…`
ZINC5759636 ZINC	0.810	324.4 Da LogP 0.24 TPSA 132.9	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)[C@H](O)[C@H](N)Cc1ccc(O)cc1)…`
ZINC2390944 ZINC	0.756	278.4 Da LogP 1.17 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)[C@@H](N)Cc1ccccc1)C(=O)O`
ZINC6049599 ZINC	0.756	278.4 Da LogP 1.17 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)C[C@@H](NC(=O)[C@@H](N)Cc1ccccc1)C(=O)O`
ZINC2391109 ZINC	0.750	307.3 Da LogP 1.55 TPSA 103.7	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)[C@@H](Cc1ccccc1)C(=O)O)C(=O)O`
ZINC27727766 ZINC	0.750	307.3 Da LogP 1.55 TPSA 103.7	✓ Ro5	✓ Clean	`CC(C)C[C@@H](NC(=O)[C@@H](Cc1ccccc1)C(=O)O)C(=O…`
ZINC27727773 ZINC	0.750	307.3 Da LogP 1.55 TPSA 103.7	✓ Ro5	✓ Clean	`CC(C)C[C@@H](NC(=O)[C@H](Cc1ccccc1)C(=O)O)C(=O)O`
ZINC4899476 ZINC	0.750	307.3 Da LogP 1.55 TPSA 103.7	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)[C@H](Cc1ccccc1)C(=O)O)C(=O)O`
ZINC27644022 ZINC	0.721	294.4 Da LogP 0.29 TPSA 112.6	✓ Ro5	✓ Clean	`CCC[C@H](NC(=O)[C@H](O)[C@H](N)Cc1ccccc1)C(=O)O`
ZINC6003711 ZINC	0.711	441.5 Da LogP 0.87 TPSA 141.7	✓ Ro5	✓ Clean	`CC(C)[C@H](NC(=O)[C@@H](O)[C@H](N)Cc1ccccc1)C(=…`
ZINC38212936 ZINC	0.711	231.3 Da LogP 0.72 TPSA 46.6	✓ Ro5	✓ Clean	`COC(=O)[C@@H]1CCCN1C(=O)[C@H](C)CS`
ZINC111451008 ZINC	0.703	231.3 Da LogP 1.06 TPSA 57.6	✓ Ro5	✓ Clean	`CSC[C@H](C)C(=O)N1CCC[C@H]1C(=O)O`
ZINC6036727 ZINC	0.703	231.3 Da LogP 1.06 TPSA 57.6	✓ Ro5	✓ Clean	`CSC[C@@H](C)C(=O)N1CCC[C@H]1C(=O)O`
ZINC237154739 ZINC	0.684	215.2 Da LogP 0.34 TPSA 66.8	✓ Ro5	✓ Clean	`COC[C@@H](C)C(=O)N1CCC[C@H]1C(=O)O`
ZINC237231340 ZINC	0.684	215.2 Da LogP 0.34 TPSA 66.8	✓ Ro5	✓ Clean	`COC[C@H](C)C(=O)N1CCC[C@H]1C(=O)O`
ZINC4899773 ZINC	0.682	391.5 Da LogP 1.70 TPSA 121.5	✓ Ro5	✓ Clean	`CC(C)C[C@H](N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](…`
ZINC1569745 ZINC	0.674	278.4 Da LogP 1.17 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)C[C@H](N)C(=O)N[C@@H](Cc1ccccc1)C(=O)O`
ZINC1569746 ZINC	0.674	278.4 Da LogP 1.17 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)C[C@@H](N)C(=O)N[C@@H](Cc1ccccc1)C(=O)O`
ZINC1569747 ZINC	0.674	278.4 Da LogP 1.17 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)C[C@H](N)C(=O)N[C@H](Cc1ccccc1)C(=O)O`
ZINC1569748 ZINC	0.674	278.4 Da LogP 1.17 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)C[C@@H](N)C(=O)N[C@H](Cc1ccccc1)C(=O)O`
ZINC67664984 ZINC	0.667	247.3 Da LogP 0.08 TPSA 74.7	✓ Ro5	✓ Clean	`C[C@H](C[S@](C)=O)C(=O)N1CCC[C@H]1C(=O)O`
ZINC67664986 ZINC	0.667	247.3 Da LogP 0.08 TPSA 74.7	✓ Ro5	✓ Clean	`C[C@H](C[S@@](C)=O)C(=O)N1CCC[C@H]1C(=O)O`
ZINC2983230 ZINC	0.659	320.4 Da LogP 1.35 TPSA 95.5	✓ Ro5	✓ Clean	`CC(=O)N[C@H](Cc1ccccc1)C(=O)N[C@@H](CC(C)C)C(=O…`
ZINC2983231 ZINC	0.659	320.4 Da LogP 1.35 TPSA 95.5	✓ Ro5	✓ Clean	`CC(=O)N[C@H](Cc1ccccc1)C(=O)N[C@H](CC(C)C)C(=O)O`
ZINC2983232 ZINC	0.659	320.4 Da LogP 1.35 TPSA 95.5	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](CC(C)C)C(=…`
ZINC2983233 ZINC	0.659	320.4 Da LogP 1.35 TPSA 95.5	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@H](CC(C)C)C(=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.