KpATCC43816 Protein target profile

bacterial extracellular solute-binding, 5 Middlefamily protein

Accession: VK055_0456

Gene: AIK79082.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A0H3GQV3

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Length 567

Pocket druggability (P2Rank · AlphaFold DB model) 0.853

Direct ligand evidence 0 54 total records

Functional annotation 0 EC 5 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

Risks to review

Evidence coverage

Core evidence streams are available for this target.

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: 0.5% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 26.374 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 92.6 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) 0.853

Structure A0A0H3GQV3

Pocket Pocket 1

Druggability (FPocket) 0.602

Structure A0A0H3GQV3

Pocket Pocket 29

ColabFold model

P2Rank 0.759 · Pocket 1

FPocket 0.122 · Pocket 2

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 26 / 4744 genomes with a hit

Prevalence 0.5%

Metabolic context

Reactions catalyzed, pathway membership, and centrality in the genome-scale metabolic network.

This protein is not associated with the imported metabolic network for this genome.

Browse the genome's metabolic network

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MSRLQQGLKTRQTRFALALKVALLGGVVAFSSAVFAEGLLKEGITPATDASQIPASAKLRKDTVVAGISEPQGIFNPYFFVNGWDENVTNVIFSRLIDWDSQGKLVPGLAESWTVSPDNKVYTIKLRPGLTFSDGSPLTAEDVAFTLTVLLDPKYDGDTDITLANIAGGTDYKAGKADSVSGLKVIDPLTLQVTTTQPGATTLAKIGGPVLSKAWYGKGYQRGNLDYLRSLHGKPLGNGPYVYDKYIPGQEIRFHANSHFYRGTPPTPRFIYRVTNPSTNFQLFQTGETDYDAFTSRPDDIEQLKMLGFANINLYGSSDYSQVEFNVHRPALQDKRVRQALIYGLDRQKLIDVVYQGYGKVAIEPIAPISWAFNAEGVNPYPYDPAQAKKLLDEAGWKAGADGIRAKDGQRLELTLLVSKKVLNDALIPIAKENWRQIGVLLKPQVVDFNALMAQRKAGNYDLASFSTSTLNDPHDGVWDFYSSEAKESGYHNAEVDKLINAGNAVLDIEQRKPIYHQLYKVLADDPPVILLGYREILSASSARVSGFKPDIYNGLTGSLPDVKIVK

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

5 GO

Subcellular localization

Localization: Periplasmic

Gene Ontology (GO)

GO:0043190 A complex for the transport of metabolites into and out of the cell, typically comprised of four domains; two membrane-associated domains and two ATP-binding domains at the intracellular face of the membrane, that form a central pore through the plasma membrane. Each of the four core domains may be encoded as a separate polypeptide or the domains can be fused in any one of a number of ways into multidomain polypeptides. In Bacteria and Archaebacteria, ABC transporters also include substrate binding proteins to bind substrate external to the cytoplasm and deliver it to the transporter.
GO:0055085 The process in which a solute is transported across a lipid bilayer, from one side of a membrane to the other.
GO:0030288 The region between the inner (cytoplasmic or plasma) membrane and outer membrane of organisms with two membranes such as Gram negative bacteria. These periplasmic spaces are relatively thick and contain a thin peptidoglycan layer (PGL), also referred to as a thin cell wall.
GO:1904680 Enables the transfer of a peptide from one side of a membrane to the other.
GO:0015833 The directed movement of peptides, compounds of two or more amino acids where the alpha carboxyl group of one is bound to the alpha amino group of another, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

17 records

Show feature table

Start	End	DB	Term	Name
104	486	Pfam	PF00496	Bacterial extracellular solute-binding proteins, family 5 Middle
104	486	InterPro	IPR000914	Solute-binding protein family 5 domain
63	548	CDD	cd00995	PBP2_NikA_DppA_OppA_like
319	534	Gene3D	G3DSA:3.10.105.10	-
37	567	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
29	36	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
15	555	PANTHER	PTHR30290	PERIPLASMIC BINDING COMPONENT OF ABC TRANSPORTER
15	555	InterPro	IPR039424	Solute-binding protein family 5
15	28	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
74	549	Gene3D	G3DSA:3.40.190.10	-
13	35	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
20	559	PIRSF	PIRSF002741	MppA
20	559	InterPro	IPR030678	Peptide/nickel binding protein, MppA-type
1	14	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
1	36	Phobius	SIGNAL_PEPTIDE	Signal peptide region
93	225	Gene3D	G3DSA:3.90.76.10	-
60	555	SUPERFAMILY	SSF53850	Periplasmic binding protein-like II

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

0.853

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Surrounding area

Pocket 2 P2Rank #2

0.821

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Surrounding area

Pocket 3 P2Rank #3

0.265

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Surrounding area

Pocket 4 P2Rank #4

0.194

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Surrounding area

Pocket 5 P2Rank #5

0.092

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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 #29

0.602

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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

0.759

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Surrounding area

Pocket 2 P2Rank #2

0.626

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Surrounding area

Pocket 3 P2Rank #3

0.448

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Surrounding area

Pocket 4 P2Rank #4

0.447

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Surrounding area

Pocket 5 P2Rank #5

0.072

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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_A0A0H3GQV3	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_0456	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

EDT PDB via homolog 292.2 Da · LogP -2.07 · TPSA 155.7 Open detail RCSB PDB

GDS PDB via homolog Detail RCSB PDB

MLI PDB via homolog Detail RCSB PDB

OXL PDB via homolog Detail RCSB PDB

ZINC19364242 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
EDT RCSB PDB	4OES	Q9AL82	292.2 Da LogP -2.07 TPSA 155.7	✓ Ro5	✓ Clean	`C(CN(CC(=O)O)CC(=O)O)N(CC(=O)O)CC(=O)O`
GDS RCSB PDB	3M8U	B8F653	612.6 Da LogP -3.88 TPSA 317.6	3 viol.	✓ Clean	`C(CC(=O)N[C@@H](CSSC[C@@H](C(=O)NCC(=O)O)NC(=O)…`
MLI RCSB PDB	3M8U	B8F653	102.0 Da LogP -3.12 TPSA 80.3	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(=O)[O-]`
OXL RCSB PDB	4OEV	Q0P844	88.0 Da LogP -3.51 TPSA 80.3	✓ Ro5	✓ Clean	`C(=O)(C(=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).

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
ZINC19364242 ZINC	1.000	292.2 Da LogP -2.07 TPSA 155.7	✓ Ro5	✓ Clean	`O=C(O)CN(CCN(CC(=O)O)CC(=O)O)CC(=O)O`
ZINC19419017 ZINC	0.933	393.3 Da LogP -2.68 TPSA 196.2	✓ Ro5	✓ Clean	`O=C(O)CN(CCN(CC(=O)O)CC(=O)O)CCN(CC(=O)O)CC(=O)O`
ZINC22593216 ZINC	0.933	494.5 Da LogP -3.30 TPSA 236.8	1 viol.	✓ Clean	`O=C(O)CN(CCN(CCN(CC(=O)O)CC(=O)O)CC(=O)O)CCN(CC…`
ZINC31350707 ZINC	0.767	349.4 Da LogP -1.86 TPSA 175.9	✓ Ro5	✓ Clean	`CC(=O)SC[C@@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)NCC…`
ZINC31350710 ZINC	0.767	349.4 Da LogP -1.86 TPSA 175.9	✓ Ro5	✓ Clean	`CC(=O)SC[C@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)NCC(…`
ZINC31350713 ZINC	0.767	349.4 Da LogP -1.86 TPSA 175.9	✓ Ro5	✓ Clean	`CC(=O)SC[C@@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NCC(…`
ZINC3872733 ZINC	0.767	336.3 Da LogP -1.72 TPSA 188.2	✓ Ro5	✓ Clean	`N[C@H](CCC(=O)N[C@@H](CSN=O)C(=O)NCC(=O)O)C(=O)O`
ZINC3872734 ZINC	0.767	336.3 Da LogP -1.72 TPSA 188.2	✓ Ro5	✓ Clean	`N[C@H](CCC(=O)N[C@H](CSN=O)C(=O)NCC(=O)O)C(=O)O`
ZINC4544082 ZINC	0.767	335.4 Da LogP -1.38 TPSA 158.8	✓ Ro5	✓ Clean	`CCSC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC4544083 ZINC	0.767	335.4 Da LogP -1.38 TPSA 158.8	✓ Ro5	✓ Clean	`CCSC[C@@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC1769289 ZINC	0.765	306.3 Da LogP -1.68 TPSA 155.7	✓ Ro5	✓ Clean	`O=C(O)CN(CCCN(CC(=O)O)CC(=O)O)CC(=O)O`
ZINC4683946 ZINC	0.765	320.3 Da LogP -1.29 TPSA 155.7	✓ Ro5	✓ Clean	`O=C(O)CN(CCCCN(CC(=O)O)CC(=O)O)CC(=O)O`
ZINC19364891 ZINC	0.737	204.2 Da LogP -0.98 TPSA 81.1	✓ Ro5	✓ Clean	`CN(C)CCN(CC(=O)O)CC(=O)O`
ZINC19364892 ZINC	0.737	232.3 Da LogP -0.20 TPSA 81.1	✓ Ro5	✓ Clean	`CCN(CC)CCN(CC(=O)O)CC(=O)O`
ZINC19366122 ZINC	0.737	278.3 Da LogP -2.16 TPSA 138.6	✓ Ro5	✓ Clean	`O=C(O)CN(CCO)CCN(CC(=O)O)CC(=O)O`
ZINC33806192 ZINC	0.737	320.3 Da LogP -1.29 TPSA 155.7	✓ Ro5	✓ Clean	`O=C(O)CCN(CCC(=O)O)CCN(CC(=O)O)CC(=O)O`
ZINC5908834 ZINC	0.737	379.3 Da LogP -2.09 TPSA 196.2	✓ Ro5	✓ Clean	`O=C(O)CN(CCN(CCN(CC(=O)O)CC(=O)O)C(=O)O)CC(=O)O`
ZINC2554974 ZINC	0.732	289.3 Da LogP -1.73 TPSA 158.8	✓ Ro5	✓ Clean	`CC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC3830891 ZINC	0.732	307.3 Da LogP -2.21 TPSA 158.8	1 viol.	✓ Clean	`N[C@@H](CCC(=O)N[C@@H](CS)C(=O)NCC(=O)O)C(=O)O`
ZINC3830892 ZINC	0.732	307.3 Da LogP -2.21 TPSA 158.8	1 viol.	✓ Clean	`N[C@@H](CCC(=O)N[C@H](CS)C(=O)NCC(=O)O)C(=O)O`
ZINC3830893 ZINC	0.732	307.3 Da LogP -2.21 TPSA 158.8	1 viol.	✓ Clean	`N[C@H](CCC(=O)N[C@@H](CS)C(=O)NCC(=O)O)C(=O)O`
ZINC3830894 ZINC	0.732	307.3 Da LogP -2.21 TPSA 158.8	1 viol.	✓ Clean	`N[C@H](CCC(=O)N[C@H](CS)C(=O)NCC(=O)O)C(=O)O`
ZINC2527900 ZINC	0.722	205.2 Da LogP -1.07 TPSA 115.1	✓ Ro5	✓ Clean	`O=C(O)CCN(CC(=O)O)CC(=O)O`
ZINC4261886 ZINC	0.722	348.4 Da LogP -0.51 TPSA 155.7	✓ Ro5	✓ Clean	`O=C(O)CN(CCCCCCN(CC(=O)O)CC(=O)O)CC(=O)O`
ZINC22057269 ZINC	0.702	406.5 Da LogP -0.94 TPSA 179.1	✓ Ro5	✓ Clean	`CCN(CC)C(=O)SC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O…`
ZINC35997292 ZINC	0.702	406.5 Da LogP -0.94 TPSA 179.1	✓ Ro5	✓ Clean	`CCN(CC)C(=O)SC[C@H](NC(=O)CC[C@@H](N)C(=O)O)C(=…`
ZINC4534315 ZINC	0.702	363.4 Da LogP -0.60 TPSA 158.8	✓ Ro5	✓ Clean	`CCCCSC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC98091813 ZINC	0.702	406.5 Da LogP -0.94 TPSA 179.1	✓ Ro5	✓ Clean	`CCN(CC)C(=O)SC[C@@H](NC(=O)CC[C@H](N)C(=O)O)C(=…`
ZINC98091814 ZINC	0.702	406.5 Da LogP -0.94 TPSA 179.1	✓ Ro5	✓ Clean	`CCN(CC)C(=O)SC[C@@H](NC(=O)CC[C@@H](N)C(=O)O)C(…`
ZINC149813449 ZINC	0.700	278.2 Da LogP -1.48 TPSA 155.7	✓ Ro5	✓ Clean	`O=C(O)CN(CCN(CC(=O)O)C(=O)O)CC(=O)O`
ZINC22576460 ZINC	0.684	320.3 Da LogP -1.29 TPSA 155.7	✓ Ro5	✓ Clean	`O=C(O)CCN(CCN(CCC(=O)O)CC(=O)O)CC(=O)O`
ZINC1616624 ZINC	0.682	355.3 Da LogP -3.25 TPSA 213.2	1 viol.	✓ Clean	`N[C@@H](CCC(=O)N[C@@H](CS(=O)(=O)O)C(=O)NCC(=O)…`
ZINC1616625 ZINC	0.682	355.3 Da LogP -3.25 TPSA 213.2	1 viol.	✓ Clean	`N[C@@H](CCC(=O)N[C@H](CS(=O)(=O)O)C(=O)NCC(=O)O…`
ZINC1616626 ZINC	0.682	355.3 Da LogP -3.25 TPSA 213.2	1 viol.	✓ Clean	`N[C@H](CCC(=O)N[C@@H](CS(=O)(=O)O)C(=O)NCC(=O)O…`
ZINC1616627 ZINC	0.682	355.3 Da LogP -3.25 TPSA 213.2	1 viol.	✓ Clean	`N[C@H](CCC(=O)N[C@H](CS(=O)(=O)O)C(=O)NCC(=O)O)…`
ZINC14880561 ZINC	0.673	419.5 Da LogP 0.96 TPSA 158.8	✓ Ro5	✓ Clean	`CCCCCCCCSC[C@@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)N…`
ZINC14880563 ZINC	0.673	419.5 Da LogP 0.96 TPSA 158.8	✓ Ro5	✓ Clean	`CCCCCCCCSC[C@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)NC…`
ZINC14880565 ZINC	0.673	419.5 Da LogP 0.96 TPSA 158.8	✓ Ro5	✓ Clean	`CCCCCCCCSC[C@@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NC…`
ZINC3874923 ZINC	0.673	391.5 Da LogP 0.18 TPSA 158.8	✓ Ro5	✓ Clean	`CCCCCCSC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NCC(=…`
ZINC3874924 ZINC	0.673	391.5 Da LogP 0.18 TPSA 158.8	✓ Ro5	✓ Clean	`CCCCCCSC[C@@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NCC(…`
ZINC3874925 ZINC	0.673	391.5 Da LogP 0.18 TPSA 158.8	✓ Ro5	✓ Clean	`CCCCCCSC[C@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)NCC(…`
ZINC3874926 ZINC	0.673	391.5 Da LogP 0.18 TPSA 158.8	✓ Ro5	✓ Clean	`CCCCCCSC[C@@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)NCC…`
ZINC90669676 ZINC	0.667	377.4 Da LogP -2.57 TPSA 176.0	✓ Ro5	✓ Clean	`O=CCN(CCN(CC(=O)O)CC(=O)O)CCN(CC(=O)O)CC(=O)O`
ZINC2390999 ZINC	0.655	275.3 Da LogP -1.99 TPSA 172.8	✓ Ro5	✓ Clean	`NC(=O)CC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)O`
ZINC22052182 ZINC	0.650	336.3 Da LogP -2.05 TPSA 164.9	✓ Ro5	✓ Clean	`O=C(O)CN(CCOCCN(CC(=O)O)CC(=O)O)CC(=O)O`
ZINC4962382 ZINC	0.647	425.5 Da LogP -0.52 TPSA 175.9	✓ Ro5	✓ Clean	`N[C@H](CCC(=O)N[C@@H](CSCC(=O)c1ccccc1)C(=O)NCC…`
ZINC4962383 ZINC	0.647	425.5 Da LogP -0.52 TPSA 175.9	✓ Ro5	✓ Clean	`N[C@H](CCC(=O)N[C@H](CSCC(=O)c1ccccc1)C(=O)NCC(…`
ZINC4962414 ZINC	0.647	439.5 Da LogP -0.13 TPSA 175.9	✓ Ro5	✓ Clean	`N[C@@H](CCC(=O)N[C@H](CSCCC(=O)c1ccccc1)C(=O)NC…`
ZINC4962415 ZINC	0.647	439.5 Da LogP -0.13 TPSA 175.9	✓ Ro5	✓ Clean	`N[C@H](CCC(=O)N[C@@H](CSCCC(=O)c1ccccc1)C(=O)NC…`
ZINC4962416 ZINC	0.647	439.5 Da LogP -0.13 TPSA 175.9	✓ Ro5	✓ Clean	`N[C@H](CCC(=O)N[C@H](CSCCC(=O)c1ccccc1)C(=O)NCC…`

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 A0A0H3GQV3