KpKP13 Protein target profile

D-alanyl-D-alanine carboxypeptidase dacD

Accession: KP13_05419

Gene: dacD AHE43707.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GV65

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Length 389

Pocket druggability (P2Rank · AlphaFold DB model) 0.28

Direct ligand evidence 0 65 total records

Functional annotation 1 EC 8 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 0.55. 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: 2.3% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 44.909 Higher values support similarity to known essential genes.
DEG E-value: 1.49e-116 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 91.03 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) 0.28

Structure A0A0H3GV65

Pocket Pocket 1

Druggability (FPocket) 0.551

Structure A0A0H3GV65

Pocket Pocket 13

ColabFold model

P2Rank 0.16 · Pocket 1

FPocket 0.172 · Pocket 17

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 110 / 4744 genomes with a hit

Prevalence 2.3%

Sequence

Primary amino-acid sequence viewer.

MPLKGRLFIAVSLLASSVSCAFAVDLPATVAPPSIQAGSWVLMDYTTGQVLTAGNEHQQRNPASLTKLMTGYVVDRAIDSHRITFDDIVTVGKDAWAKGNPVFDGSSLMFLKPGDRVSVRDLSRGLIVDSGNDACVALADYVAGGQPQFVALMNQYVEKLHLRDTHFETVHGLDAPGQHSSAYDLAVLSRAIIHGEPDVYHMYSQKSLTWNGITQQNRNGLLWDKTMNVDGLKTGHTSGAGFNLIASAVDGQRRLIAVVMGADSPKGREQQAAKLLHWGQQNFDTVQVLQKGQKVGTERIWYGDKEQIKLGTDQDFWLALPKAEVSRIKAKYVLDKKDLEAPIAANQRVGEISLYDGDKVVGHYPLVTLESINKGGVFSRMSDYLHHEL

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Subcellular localization

Localization: CytoplasmicMembrane

Enzyme Commission (EC)

3.4.16.4

Gene Ontology (GO)

GO:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
GO:0009002 Catalysis of the reaction: (Ac)2-L-Lys-D-alanyl-D-alanine + H2O = (Ac)2-L-Lys-D-alanine + D-alanine.
GO:0004180 Catalysis of the hydrolysis of a single C-terminal amino acid residue from a polypeptide chain.
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:0008658 Binding to penicillin, an antibiotic that contains the condensed beta-lactamthiazolidine ring system.
GO:0071555 A process that results in the assembly, arrangement of constituent parts, or disassembly of the cell wall, the rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal and most prokaryotic cells, maintaining their shape and protecting them from osmotic lysis.
GO:0009252 The chemical reactions and pathways resulting in the formation of peptidoglycans, any of a class of glycoconjugates found in bacterial cell walls and consisting of long glycan strands of alternating residues of beta-(1,4) linked N-acetylglucosamine and N-acetylmuramic acid, cross-linked by short peptides.
GO:0008360 Any process that modulates the surface configuration of a cell.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

29 records

Show feature table

Start	End	DB	Term	Name
283	373	Gene3D	G3DSA:2.60.410.10	-
283	373	InterPro	IPR037167	D-Ala-D-Ala carboxypeptidase, C-terminal domain superfamily
34	287	PANTHER	PTHR21581	D-ALANYL-D-ALANINE CARBOXYPEPTIDASE
1	23	SignalP_GRAM_POSITIVE	SignalP-TM	SignalP-TM
8	283	SUPERFAMILY	SSF56601	beta-lactamase/transpeptidase-like
8	283	InterPro	IPR012338	Beta-lactamase/transpeptidase-like
283	376	SUPERFAMILY	SSF69189	Penicillin-binding protein associated domain
283	376	InterPro	IPR015956	Penicillin-binding protein, C-terminal domain superfamily
1	23	Phobius	SIGNAL_PEPTIDE	Signal peptide region
1	23	SignalP_GRAM_NEGATIVE	SignalP-noTM	SignalP-noTM
24	389	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
1	20	ProSiteProfiles	PS51257	Prokaryotic membrane lipoprotein lipid attachment site profile.
1	6	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
122	139	PRINTS	PR00725	D-Ala-D-Ala carboxypeptidase 1 (S11) family signature
122	139	InterPro	IPR018044	Peptidase S11, D-alanyl-D-alanine carboxypeptidase A
63	74	PRINTS	PR00725	D-Ala-D-Ala carboxypeptidase 1 (S11) family signature
63	74	InterPro	IPR018044	Peptidase S11, D-alanyl-D-alanine carboxypeptidase A
149	162	PRINTS	PR00725	D-Ala-D-Ala carboxypeptidase 1 (S11) family signature
149	162	InterPro	IPR018044	Peptidase S11, D-alanyl-D-alanine carboxypeptidase A
21	282	FunFam	G3DSA:3.40.710.10:FF:000001	D-alanyl-D-alanine serine-type carboxypeptidase
7	18	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
283	374	SMART	SM00936	PBP5_C_2
283	374	InterPro	IPR012907	Peptidase S11, D-Ala-D-Ala carboxypeptidase A, C-terminal
29	263	Pfam	PF00768	D-alanyl-D-alanine carboxypeptidase
29	263	InterPro	IPR001967	Peptidase S11, D-alanyl-D-alanine carboxypeptidase A, N-terminal
283	374	Pfam	PF07943	Penicillin-binding protein 5, C-terminal domain
14	282	Gene3D	G3DSA:3.40.710.10	-
14	282	InterPro	IPR012338	Beta-lactamase/transpeptidase-like
19	23	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.

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

0.28

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Surrounding area

Pocket 2 P2Rank #2

0.036

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Surrounding area

Pocket 3 P2Rank #3

0.009

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Surrounding area

Pocket 4 P2Rank #4

0.001

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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 #13

0.551

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Surrounding area

Residue sets

UniProt: Active site:24-24 Acyl-ester intermediate

UniProt: Active site:27-27 Proton acceptor

UniProt: Active site:90-90

UniProt: Binding site:193-193

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_A0A0H3GV65	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_05419	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.

65 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 15 records from similar proteins

Structural ligands 14 0 loaded crystals

Measured bioactivity 1 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

AI8 PDB via homolog 607.7 Da · LogP 1.24 · TPSA 185.7 Open detail RCSB PDB

AIC PDB via homolog Detail RCSB PDB

BO9 PDB via homolog Detail RCSB PDB

CEW PDB via homolog Detail RCSB PDB

CXV PDB via homolog Detail RCSB PDB

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
AI8 RCSB PDB	5TW4	A0A0H2WY27	607.7 Da LogP 1.24 TPSA 185.7	2 viol.	✓ Clean	`CCON=C(c1nc(sn1)N)C(=O)N[C@H](C=O)[C@@H]2NC(=C(…`
AIC RCSB PDB	3ITA	P08506	349.4 Da LogP 0.32 TPSA 112.7	✓ Ro5	✓ Clean	`CC1([C@@H](N2[C@H](S1)[C@@H](C2=O)NC(=O)[C@@H](…`
BO9 RCSB PDB	1Z6F	P0AEB2	580.4 Da LogP 0.84 TPSA 212.6	2 viol.	✓ Clean	`B([C@@H](C)NC(=O)[C@H](CCCCNC(=O)OCc1ccccc1)NC(…`
CEW RCSB PDB	3HUM	A0A0H2WY27	401.5 Da LogP -0.89 TPSA 155.1	✓ Ro5	✓ Clean	`CC1=C(N[C@H](SC1)[C@@H](C=O)NC(=O)C(=NOC)C2=CSC…`
CXV RCSB PDB	3MZD	P0AEB2	437.9 Da LogP 2.50 TPSA 121.5	✓ Ro5	✓ Clean	`Cc1c(c(no1)c2ccccc2Cl)C(=O)N[C@@H](C=O)[C@@H]3N…`
HJ2 RCSB PDB	3BEC	P0AEB2	389.4 Da LogP -0.45 TPSA 179.0	1 viol.	✓ Clean	`CC1=C(N[C@H](SC1)[C@@H](C(=O)O)NC(=O)CCCC[C@@H]…`
HJ3 RCSB PDB	3BEB	P0AEB2	375.4 Da LogP -0.46 TPSA 158.8	✓ Ro5	✓ Clean	`CC1([C@@H](N[C@H](S1)[C@@H](C=O)NC(=O)CCCC[C@@H…`
IM2 RCSB PDB	3MZF	P0AEB2	301.4 Da LogP -0.23 TPSA 122.5	✓ Ro5	✓ Clean	`[H]/N=C/NCCSC1=C(N[C@H](C1)[C@H](C=O)[C@@H](C)O…`
MXR RCSB PDB	6NTZ	P0AEB2	385.5 Da LogP -0.35 TPSA 119.3	✓ Ro5	✓ Clean	`C[C@H]1[C@@H](C(=N[C@H]1[C@H](C=O)[C@@H](C)O)C(…`
NFF RCSB PDB	5TY2	A0A0H2WY27	416.5 Da LogP 2.43 TPSA 104.7	✓ Ro5	✓ Clean	`CCOc1ccc2ccccc2c1C(=O)N[C@H](C=O)[C@@H]3N[C@H](…`
OK3 RCSB PDB	5J8X	P0AEB2	357.2 Da LogP 0.04 TPSA 142.1	✓ Ro5	✓ Clean	`[B-]1([C@H](Cc2cccc(c2O1)C(=O)O)NC(=O)c3ccc(cc3…`
RB6 RCSB PDB	5TX9	A0A0H2WY27	536.6 Da LogP -1.50 TPSA 212.2	3 viol.	✓ Clean	`C1CNC[C@@H]1N2CC=C(C2=O)CC3=C(N[C@H](SC3)[C@@H]…`
SIN RCSB PDB	4K91	A0A0H2ZFH3	118.1 Da LogP -0.06 TPSA 74.6	✓ Ro5	✓ Clean	`C(CC(=O)O)C(=O)O`
ZZ7 RCSB PDB	3HUN	A0A0H2WY27	367.4 Da LogP 0.15 TPSA 141.8	✓ Ro5	✓ Clean	`CC1([C@@H](N[C@H](S1)[C@@H](C(=O)O)NC(=O)[C@@H]…`

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
CHEMBL520642 ChEMBL	A0A0H2WY27	—	534.6 Da LogP -1.44 TPSA 203.4	2 viol.	✓ Clean	`Nc1nc(/C(=N/O)C(=O)N[C@@H]2C(=O)N3C(C(=O)O)=C(/…`

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
ZINC13704471 ZINC	1.000	349.4 Da LogP 0.32 TPSA 112.7	✓ Ro5	✓ Clean	`CC1(C)S[C@H]2[C@H](NC(=O)[C@@H](N)c3ccccc3)C(=O…`
ZINC1607283 ZINC	1.000	349.4 Da LogP 0.32 TPSA 112.7	✓ Ro5	✓ Clean	`CC1(C)S[C@H]2[C@H](NC(=O)[C@H](N)c3ccccc3)C(=O)…`
ZINC255982699 ZINC	1.000	367.4 Da LogP 0.15 TPSA 141.8	✓ Ro5	✓ Clean	`CC1(C)S[C@H]([C@H](NC(=O)[C@@H](N)c2ccccc2)C(=O…`
ZINC2568903 ZINC	1.000	349.4 Da LogP 0.32 TPSA 112.7	✓ Ro5	✓ Clean	`CC1(C)S[C@@H]2[C@@H](NC(=O)[C@H](N)c3ccccc3)C(=…`
ZINC3649954 ZINC	1.000	349.4 Da LogP 0.32 TPSA 112.7	✓ Ro5	✓ Clean	`CC1(C)S[C@@H]2[C@@H](NC(=O)[C@@H](N)c3ccccc3)C(…`
ZINC3830217 ZINC	1.000	349.4 Da LogP 0.32 TPSA 112.7	✓ Ro5	✓ Clean	`CC1(C)S[C@H]2[C@H](NC(=O)[C@H](N)c3ccccc3)C(=O)…`
ZINC3830218 ZINC	1.000	349.4 Da LogP 0.32 TPSA 112.7	✓ Ro5	✓ Clean	`CC1(C)S[C@@H]2[C@H](NC(=O)[C@H](N)c3ccccc3)C(=O…`
ZINC3830219 ZINC	1.000	349.4 Da LogP 0.32 TPSA 112.7	✓ Ro5	✓ Clean	`CC1(C)S[C@@H]2[C@H](NC(=O)[C@H](N)c3ccccc3)C(=O…`
ZINC4062610 ZINC	1.000	349.4 Da LogP 0.32 TPSA 112.7	✓ Ro5	✓ Clean	`CC1(C)S[C@@H]2[C@H](NC(=O)[C@@H](N)c3ccccc3)C(=…`
ZINC4523361 ZINC	1.000	349.4 Da LogP 0.32 TPSA 112.7	✓ Ro5	✓ Clean	`CC1(C)S[C@H]2[C@@H](NC(=O)[C@@H](N)c3ccccc3)C(=…`
ZINC5497159 ZINC	1.000	349.4 Da LogP 0.32 TPSA 112.7	✓ Ro5	✓ Clean	`CC1(C)S[C@@H]2[C@H](NC(=O)[C@@H](N)c3ccccc3)C(=…`
ZINC1821981 ZINC	0.840	365.4 Da LogP 0.02 TPSA 133.0	✓ Ro5	✓ Clean	`CC1(C)S[C@@H]2[C@@H](NC(=O)[C@@H](N)c3ccc(O)cc3…`
ZINC2140544 ZINC	0.840	365.4 Da LogP 0.02 TPSA 133.0	✓ Ro5	✓ Clean	`CC1(C)S[C@@H]2[C@@H](NC(=O)[C@H](N)c3ccc(O)cc3)…`
ZINC3604143 ZINC	0.840	365.4 Da LogP 0.02 TPSA 133.0	✓ Ro5	✓ Clean	`CC1(C)S[C@H]2[C@H](NC(=O)[C@H](N)c3ccc(O)cc3)C(…`
ZINC3604145 ZINC	0.840	365.4 Da LogP 0.02 TPSA 133.0	✓ Ro5	✓ Clean	`CC1(C)S[C@H]2[C@H](NC(=O)[C@H](N)c3ccc(O)cc3)C(…`
ZINC3604147 ZINC	0.840	365.4 Da LogP 0.02 TPSA 133.0	✓ Ro5	✓ Clean	`CC1(C)S[C@H]2[C@H](NC(=O)[C@@H](N)c3ccc(O)cc3)C…`
ZINC3830215 ZINC	0.840	365.4 Da LogP 0.02 TPSA 133.0	✓ Ro5	✓ Clean	`CC1(C)S[C@@H]2[C@H](NC(=O)[C@H](N)c3ccc(O)cc3)C…`
ZINC3830216 ZINC	0.840	365.4 Da LogP 0.02 TPSA 133.0	✓ Ro5	✓ Clean	`CC1(C)S[C@@H]2[C@H](NC(=O)[C@H](N)c3ccc(O)cc3)C…`
ZINC3978046 ZINC	0.840	365.4 Da LogP 0.02 TPSA 133.0	✓ Ro5	✓ Clean	`CC1(C)S[C@@H]2[C@H](NC(=O)[C@@H](N)c3ccc(O)cc3)…`
ZINC4042226 ZINC	0.840	365.4 Da LogP 0.02 TPSA 133.0	✓ Ro5	✓ Clean	`CC1(C)S[C@@H]2[C@H](NC(=O)[C@@H](N)c3ccc(O)cc3)…`
ZINC4534050 ZINC	0.840	365.4 Da LogP 0.02 TPSA 133.0	✓ Ro5	✓ Clean	`CC1(C)S[C@H]2[C@@H](NC(=O)[C@@H](N)c3ccc(O)cc3)…`
ZINC5496946 ZINC	0.840	365.4 Da LogP 0.02 TPSA 133.0	✓ Ro5	✓ Clean	`CC1(C)S[C@H]2[C@@H](NC(=O)[C@H](N)c3ccc(O)cc3)C…`
ZINC11616718 ZINC	0.765	378.4 Da LogP 0.49 TPSA 124.0	✓ Ro5	✓ Clean	`CC1(C)S[C@@H]2[C@H](NC(=O)[C@@H](C(=O)O)c3ccccc…`
ZINC3871878 ZINC	0.765	378.4 Da LogP 0.49 TPSA 124.0	✓ Ro5	✓ Clean	`CC1(C)S[C@H]2[C@H](NC(=O)[C@H](C(=O)O)c3ccccc3)…`
ZINC3871879 ZINC	0.765	378.4 Da LogP 0.49 TPSA 124.0	✓ Ro5	✓ Clean	`CC1(C)S[C@H]2[C@H](NC(=O)[C@H](C(=O)O)c3ccccc3)…`
ZINC3871880 ZINC	0.765	378.4 Da LogP 0.49 TPSA 124.0	✓ Ro5	✓ Clean	`CC1(C)S[C@@H]2[C@H](NC(=O)[C@H](C(=O)O)c3ccccc3…`
ZINC3871881 ZINC	0.765	378.4 Da LogP 0.49 TPSA 124.0	✓ Ro5	✓ Clean	`CC1(C)S[C@@H]2[C@H](NC(=O)[C@H](C(=O)O)c3ccccc3…`
ZINC3978033 ZINC	0.765	378.4 Da LogP 0.49 TPSA 124.0	✓ Ro5	✓ Clean	`CC1(C)S[C@@H]2[C@H](NC(=O)[C@@H](C(=O)O)c3ccccc…`
ZINC4535674 ZINC	0.765	378.4 Da LogP 0.49 TPSA 124.0	✓ Ro5	✓ Clean	`CC1(C)S[C@H]2[C@@H](NC(=O)[C@H](C(=O)O)c3ccccc3…`
ZINC4535676 ZINC	0.765	378.4 Da LogP 0.49 TPSA 124.0	✓ Ro5	✓ Clean	`CC1(C)S[C@H]2[C@@H](NC(=O)[C@@H](C(=O)O)c3ccccc…`
ZINC9212287 ZINC	0.765	378.4 Da LogP 0.49 TPSA 124.0	✓ Ro5	✓ Clean	`CC1(C)S[C@H]2[C@H](NC(=O)[C@@H](C(=O)O)c3ccccc3…`
ZINC3874216 ZINC	0.755	361.4 Da LogP 1.06 TPSA 99.1	✓ Ro5	✓ Clean	`C=N[C@@H](C(=O)N[C@@H]1C(=O)N2[C@@H](C(=O)O)C(C…`
ZINC7997960 ZINC	0.755	361.4 Da LogP 1.06 TPSA 99.1	✓ Ro5	✓ Clean	`C=N[C@H](C(=O)N[C@@H]1C(=O)N2[C@@H](C(=O)O)C(C)…`
ZINC263583677 ZINC	0.750	376.4 Da LogP 0.99 TPSA 103.8	✓ Ro5	✓ Clean	`CC(=O)[C@H](C(=O)N[C@H]1C(=O)N2[C@H]1SC(C)(C)[C…`
ZINC263583678 ZINC	0.750	376.4 Da LogP 0.99 TPSA 103.8	✓ Ro5	✓ Clean	`CC(=O)[C@H](C(=O)N[C@@H]1C(=O)N2[C@H]1SC(C)(C)[…`
ZINC4262137 ZINC	0.750	380.4 Da LogP 3.06 TPSA 114.0	✓ Ro5	✓ Clean	`CC(C)(C)OC(=O)N[C@@H](CCCCNC(=O)OCc1ccccc1)C(=O…`
ZINC4521274 ZINC	0.750	380.4 Da LogP 3.06 TPSA 114.0	✓ Ro5	✓ Clean	`CC(C)(C)OC(=O)N[C@H](CCCCNC(=O)OCc1ccccc1)C(=O)O`
ZINC71404972 ZINC	0.750	376.4 Da LogP 0.99 TPSA 103.8	✓ Ro5	✓ Clean	`CC(=O)[C@H](C(=O)N[C@H]1C(=O)N2[C@@H](C(=O)O)C(…`
ZINC71404973 ZINC	0.750	376.4 Da LogP 0.99 TPSA 103.8	✓ Ro5	✓ Clean	`CC(=O)[C@@H](C(=O)N[C@H]1C(=O)N2[C@@H](C(=O)O)C…`
ZINC71404974 ZINC	0.750	376.4 Da LogP 0.99 TPSA 103.8	✓ Ro5	✓ Clean	`CC(=O)[C@H](C(=O)N[C@@H]1C(=O)N2[C@@H](C(=O)O)C…`
ZINC71404975 ZINC	0.750	376.4 Da LogP 0.99 TPSA 103.8	✓ Ro5	✓ Clean	`CC(=O)[C@@H](C(=O)N[C@@H]1C(=O)N2[C@@H](C(=O)O)…`
ZINC256069287 ZINC	0.722	414.5 Da LogP 0.25 TPSA 141.1	✓ Ro5	✓ Clean	`CC1(C)S[C@@H]2[C@H](NC(=O)[C@H](c3ccccc3)S(=O)(…`
ZINC3875033 ZINC	0.722	414.5 Da LogP 0.25 TPSA 141.1	✓ Ro5	✓ Clean	`CC1(C)S[C@@H]2[C@H](NC(=O)[C@@H](c3ccccc3)S(=O)…`
ZINC3875034 ZINC	0.722	414.5 Da LogP 0.25 TPSA 141.1	✓ Ro5	✓ Clean	`CC1(C)S[C@@H]2[C@H](NC(=O)[C@@H](c3ccccc3)S(=O)…`
ZINC4099012 ZINC	0.722	414.5 Da LogP 0.25 TPSA 141.1	✓ Ro5	✓ Clean	`CC1(C)S[C@@H]2[C@H](NC(=O)[C@H](c3ccccc3)S(=O)(…`
ZINC146548960 ZINC	0.719	399.9 Da LogP 0.68 TPSA 133.0	✓ Ro5	✓ Clean	`CC1(C)S[C@@H]2[C@H](NC(=O)[C@H](N)c3ccc(O)c(Cl)…`
ZINC146549165 ZINC	0.719	399.9 Da LogP 0.68 TPSA 133.0	✓ Ro5	✓ Clean	`CC1(C)S[C@@H]2[C@H](NC(=O)[C@H](N)c3ccc(O)c(Cl)…`
ZINC198842276 ZINC	0.719	399.9 Da LogP 0.68 TPSA 133.0	✓ Ro5	✓ Clean	`CC1(C)S[C@@H]2[C@H](NC(=O)[C@@H](N)c3ccc(O)c(Cl…`
ZINC2382315751 ZINC	0.719	399.9 Da LogP 0.68 TPSA 133.0	✓ Ro5	✓ Clean	`CC1(C)S[C@@H]2[C@H](NC(=O)[C@@H](N)c3ccc(O)c(Cl…`
ZINC54053589 ZINC	0.714	375.4 Da LogP 1.67 TPSA 135.5	✓ Ro5	Alert	`CC1(C)S[C@@H]2[C@H](NC(=O)[C@H](N=[N+]=[N-])c3c…`

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 A0A0H3GV65

Chemistry

ChEMBL CHEMBL520642