KpKP13 Protein target profile

Nickel-binding periplasmic protein

Accession: KP13_00321

Gene: nikA AHE42230.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GX07

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Length 522

Pocket druggability (P2Rank · AlphaFold DB model) 0.88

Direct ligand evidence 0 66 total records

Functional annotation 0 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. Second pocket predictor agrees P2Rank predicted binding-site probability 0.88. 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: 0.7% 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: 93.89 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) 0.88

Structure A0A0H3GX07

Pocket Pocket 1

Druggability (FPocket) 0.193

Structure A0A0H3GX07

Pocket Pocket 7

ColabFold model

P2Rank 0.857 · Pocket 1

FPocket 0.113 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 32 / 4744 genomes with a hit

Prevalence 0.7%

Sequence

Primary amino-acid sequence viewer.

MSIIRLTLLALLACVPLLAQAAPYQLTTAWPVNVGPLNPHLYTPNQMFAQSMVYEPLVKYQADGSVQPWLATRWRHSADGKTWWFTLRDDVAFSNGEPFNAQAAAANFRAVLANRQRHAWLELANQITDVRALSATELQITLKSAYAPLLQELALPRPFRFIAPSQFIDGGTARGIKAPIGTGPWRLASSQLNQRDVLVRNERYWGRKPALQQITIKVIPDATSRAVAFETGEIDMLYGDEGLLPLDTFERFRHHPGYVARLSAPAETVMLALNASQGPTREQAVREALNYAVDKQTLVDSVLYGTQQVADTLFAPSVPYAPQDLTPRRYDPTKARALLEQAGWQQLEGQPWRQKAGQPLAIELAFIGTDALAKSMAEIIQANLRQVGVQVTLVGEEESSIYARQREGRFGMIFNRTWGAPYDPHAFLSSMRVPSHADYQAQRGLPDKALIDKEISEVLTTGDEAQRRKLYHDVLTRLHQDAVYLPISYVSLMSVARQEVGEIPFAPVTSEIPFDQITPVTP

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

8 GO

Subcellular localization

Localization: Periplasmic

Gene Ontology (GO)

GO:0016151 Binding to a nickel (Ni) cation.
GO:0015675 The directed movement of nickel (Ni) cations into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
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:0020037 Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring.
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.

20 records

Show feature table

Start	End	DB	Term	Name
3	514	PANTHER	PTHR30290	PERIPLASMIC BINDING COMPONENT OF ABC TRANSPORTER
3	514	InterPro	IPR039424	Solute-binding protein family 5
25	514	CDD	cd08489	PBP2_NikA
25	514	InterPro	IPR011980	Nickel ABC transporter, substrate-binding protein NikA
1	5	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
22	522	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
1	21	SignalP_GRAM_NEGATIVE	SignalP-noTM	SignalP-noTM
48	263	Gene3D	G3DSA:3.40.190.10	-
264	489	Gene3D	G3DSA:3.10.105.10	-
6	17	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
66	431	Pfam	PF00496	Bacterial extracellular solute-binding proteins, family 5 Middle
66	431	InterPro	IPR000914	Solute-binding protein family 5 domain
1	21	Phobius	SIGNAL_PEPTIDE	Signal peptide region
19	517	PIRSF	PIRSF002741	MppA
19	517	InterPro	IPR030678	Peptide/nickel binding protein, MppA-type
1	21	SignalP_GRAM_POSITIVE	SignalP-TM	SignalP-TM
26	508	SUPERFAMILY	SSF53850	Periplasmic binding protein-like II
18	21	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
22	517	NCBIfam	TIGR02294	nickel ABC transporter substrate-binding protein
22	517	InterPro	IPR011980	Nickel ABC transporter, substrate-binding protein NikA

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

0.88

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Surrounding area

Pocket 2 P2Rank #2

0.434

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Surrounding area

Pocket 3 P2Rank #3

0.372

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Surrounding area

Pocket 4 P2Rank #4

0.136

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Surrounding area

Pocket 5 P2Rank #5

0.078

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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

0.857

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Surrounding area

Pocket 2 P2Rank #2

0.508

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Surrounding area

Pocket 3 P2Rank #3

0.358

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Surrounding area

Pocket 4 P2Rank #4

0.102

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Surrounding area

Pocket 5 P2Rank #5

0.087

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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_A0A0H3GX07	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_00321	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.

66 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 16 records from similar proteins

Structural ligands 16 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

6RP PDB via homolog 192.2 Da · LogP 0.21 · TPSA 72.9 Open detail RCSB PDB

8UX PDB via homolog Detail RCSB PDB

9YH PDB via homolog Detail RCSB PDB

9YK PDB via homolog Detail RCSB PDB

BHN 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
6RP RCSB PDB	5L8D	P33590	192.2 Da LogP 0.21 TPSA 72.9	✓ Ro5	✓ Clean	`c1cnn(c1)C(C(=O)O)n2cccn2`
8UX RCSB PDB	5YH8	Q2FVE7	328.3 Da LogP -1.10 TPSA 164.6	1 viol.	✓ Clean	`C[C@@H](C(=O)O)N[C@@H](CCN[C@H](Cc1c[nH]cn1)C(=…`
9YH RCSB PDB	5ON0	P33590	448.5 Da LogP 2.60 TPSA 110.5	✓ Ro5	Alert	`COc1cccc(c1O)CN(CCN(Cc2ccccc2SC)CC(=O)O)CC(=O)O`
9YK RCSB PDB	5ON1	P33590	434.5 Da LogP 2.29 TPSA 121.5	✓ Ro5	Alert	`CSc1ccccc1CN(CCN(Cc2cccc(c2O)O)CC(=O)O)CC(=O)O`
BHN RCSB PDB	3MVZ	P33590	388.4 Da LogP 1.57 TPSA 121.5	✓ Ro5	Alert	`c1ccc(c(c1)C[N@@](CC[N@](Cc2ccccc2O)CC(=O)O)CC(…`
BHR RCSB PDB	3MW0	P33590	404.4 Da LogP 1.28 TPSA 141.8	✓ Ro5	Alert	`c1ccc(c(c1)C[N@@](CC[N@](Cc2cccc(c2O)O)CC(=O)O)…`
BHZ RCSB PDB	3MVW	P33590	372.4 Da LogP 1.87 TPSA 101.3	✓ Ro5	Alert	`c1ccc(cc1)C[N@@](CC[N@](Cc2ccccc2O)CC(=O)O)CC(=…`
CMO RCSB PDB	5L8D	P33590	28.0 Da LogP -0.04 TPSA 19.9	✓ Ro5	✓ Clean	`[C-]#[O+]`
DTD RCSB PDB	3MW0	P33590	152.2 Da LogP 0.10 TPSA 40.5	✓ Ro5	✓ Clean	`C1[C@@H]([C@H](CSS1)O)O`
DTT RCSB PDB	1ZLQ	P33590	154.3 Da LogP -0.43 TPSA 40.5	✓ Ro5	✓ Clean	`C([C@@H]([C@H](CS)O)O)S`
DTU RCSB PDB	3MVX	P33590	154.3 Da LogP -0.43 TPSA 40.5	✓ Ro5	✓ Clean	`C([C@H]([C@H](CS)O)O)S`
DTV RCSB PDB	3MVX	P33590	154.3 Da LogP -0.43 TPSA 40.5	✓ Ro5	✓ Clean	`C([C@H]([C@@H](CS)O)O)S`
EDT RCSB PDB	1ZLQ	P33590	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`
HCT RCSB PDB	3DP8	P33590	190.2 Da LogP 0.03 TPSA 111.9	✓ Ro5	✓ Clean	`C(CC(=O)O)[C@H](CC(=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-]`
PER RCSB PDB	3MVZ	P33590	32.0 Da LogP -2.38 TPSA 46.1	✓ Ro5	✓ Clean	`[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…`
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`
ZINC1690029 ZINC	0.750	204.2 Da LogP 0.42 TPSA 111.9	✓ Ro5	✓ Clean	`O=C(O)CCC(CCC(=O)O)C(=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`
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`
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`
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`
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`
ZINC217755395 ZINC	0.636	263.2 Da LogP -1.47 TPSA 147.8	✓ Ro5	✓ Clean	`O=NN(CCN(CC(=O)O)CC(=O)O)CC(=O)O`
ZINC16887664 ZINC	0.625	218.2 Da LogP 0.81 TPSA 111.9	✓ Ro5	✓ Clean	`O=C(O)CCC[C@@H](CCC(=O)O)C(=O)O`
ZINC16887665 ZINC	0.625	218.2 Da LogP 0.81 TPSA 111.9	✓ Ro5	✓ Clean	`O=C(O)CCC[C@H](CCC(=O)O)C(=O)O`
ZINC3861663 ZINC	0.619	380.4 Da LogP -2.04 TPSA 174.1	✓ Ro5	✓ Clean	`O=C(O)CN(CCOCCOCCN(CC(=O)O)CC(=O)O)CC(=O)O`
ZINC21297783 ZINC	0.609	419.4 Da LogP -3.36 TPSA 179.8	✓ Ro5	✓ Clean	`CNC(=O)CN(CCN(CCN(CC(=O)O)CC(=O)NC)CC(=O)O)CC(=…`
ZINC148116000 ZINC	0.593	204.2 Da LogP 0.12 TPSA 100.9	✓ Ro5	✓ Clean	`COC(=O)[C@@H](CCC(=O)O)CC(=O)O`
ZINC148116130 ZINC	0.593	204.2 Da LogP 0.12 TPSA 100.9	✓ Ro5	✓ Clean	`COC(=O)[C@H](CCC(=O)O)CC(=O)O`
ZINC1569727 ZINC	0.593	202.3 Da LogP -0.05 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)C[C@H](N)C(=O)N[C@@H](C)C(=O)O`
ZINC1569728 ZINC	0.593	202.3 Da LogP -0.05 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)C[C@@H](N)C(=O)N[C@@H](C)C(=O)O`
ZINC1569729 ZINC	0.593	202.3 Da LogP -0.05 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)C[C@H](N)C(=O)N[C@H](C)C(=O)O`
ZINC1569730 ZINC	0.593	202.3 Da LogP -0.05 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)C[C@@H](N)C(=O)N[C@H](C)C(=O)O`
ZINC139839569 ZINC	0.591	207.3 Da LogP -0.18 TPSA 77.8	✓ Ro5	✓ Clean	`CSCCN(CC(=O)O)CC(=O)O`
ZINC1587761 ZINC	0.591	246.3 Da LogP 0.19 TPSA 81.1	✓ Ro5	✓ Clean	`CCN(CC)CCCN(CC(=O)O)CC(=O)O`
ZINC4811653 ZINC	0.591	261.3 Da LogP 0.49 TPSA 115.1	✓ Ro5	✓ Clean	`O=C(O)CCCCCCN(CC(=O)O)CC(=O)O`
ZINC2522597 ZINC	0.586	246.3 Da LogP -0.60 TPSA 129.7	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)C[C@H](N)C(=O)O)C(=O)O`
ZINC22576825 ZINC	0.583	376.4 Da LogP -0.64 TPSA 122.7	✓ Ro5	✓ Clean	`CCOC(=O)CN(CCN(CC(=O)OCC)CC(=O)OCC)CC(=O)O`
ZINC34033067 ZINC	0.583	335.3 Da LogP -2.48 TPSA 167.7	✓ Ro5	✓ Clean	`O=C(O)CNCCN(CCN(CC(=O)O)CC(=O)O)CC(=O)O`
ZINC1532219 ZINC	0.571	244.3 Da LogP 0.98 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)C[C@H](N)C(=O)N[C@@H](CC(C)C)C(=O)O`
ZINC1532220 ZINC	0.571	244.3 Da LogP 0.98 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)[C@H](N)CC(C)C)C(=O)O`
ZINC1532221 ZINC	0.571	244.3 Da LogP 0.98 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)C[C@H](N)C(=O)N[C@H](CC(C)C)C(=O)O`
ZINC1532222 ZINC	0.571	244.3 Da LogP 0.98 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)C[C@@H](N)C(=O)N[C@H](CC(C)C)C(=O)O`
ZINC19408440 ZINC	0.567	202.2 Da LogP 1.56 TPSA 55.1	✓ Ro5	✓ Clean	`O=C(O)[C@@H](c1ccccc1)n1cccn1`
ZINC19408442 ZINC	0.567	202.2 Da LogP 1.56 TPSA 55.1	✓ Ro5	✓ Clean	`O=C(O)[C@H](c1ccccc1)n1cccn1`
ZINC218761239 ZINC	0.566	275.3 Da LogP 0.55 TPSA 103.8	✓ Ro5	✓ Clean	`CCc1ncc(CN[C@@H](Cc2c[nH]cn2)C(=O)O)cn1`
ZINC218761278 ZINC	0.566	275.3 Da LogP 0.55 TPSA 103.8	✓ Ro5	✓ Clean	`CCc1ncc(CN[C@H](Cc2c[nH]cn2)C(=O)O)cn1`
ZINC100069855 ZINC	0.565	301.4 Da LogP 3.38 TPSA 77.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCN(CC(=O)O)CC(=O)O`
ZINC100071599 ZINC	0.565	329.5 Da LogP 4.16 TPSA 77.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCN(CC(=O)O)CC(=O)O`
ZINC1769291 ZINC	0.565	245.3 Da LogP 1.82 TPSA 77.8	✓ Ro5	✓ Clean	`CCCCCCCCN(CC(=O)O)CC(=O)O`
ZINC22028872 ZINC	0.565	234.2 Da LogP -1.87 TPSA 127.2	✓ Ro5	✓ Clean	`O=C(O)CNCCN(CC(=O)O)CC(=O)O`
ZINC22060195 ZINC	0.565	232.3 Da LogP -0.02 TPSA 103.9	✓ Ro5	✓ Clean	`NCCCCCCN(CC(=O)O)CC(=O)O`
ZINC19815880 ZINC	0.563	213.2 Da LogP -0.24 TPSA 104.3	✓ Ro5	✓ Clean	`COC(=O)N[C@@H](Cc1c[nH]cn1)C(=O)O`
ZINC6095299 ZINC	0.563	211.3 Da LogP 0.18 TPSA 63.9	✓ Ro5	Alert	`OCCN(CCO)Cc1ccccc1O`
ZINC974512 ZINC	0.563	303.4 Da LogP 4.59 TPSA 23.5	✓ Ro5	Alert	`Oc1ccccc1CN(Cc1ccccc1)Cc1ccccc1`

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 A0A0H3GX07