Protein target profile

VK055_1043

primary amine oxidase

Genome: KpATCC43816 Gene: maoA AIK79666.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism 8 reactions UniProt A0A0H3GMJ1

Export view

Length 755

Pocket druggability 0.985

Metabolic reactions 8

Chokepoint Yes

Direct ligand evidence 0 74 total records

Functional annotation 1 EC 6 GO

Target summary

Strong target candidate with converging metabolic, structural and chemical evidence.

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

Main supporting evidence

Metabolic bottleneck Catalyzes a reaction that is the only producer or consumer of a metabolite in the imported metabolic model. Independent pocket support: FPocket + P2Rank Both predictors report a high-scoring binding site (FPocket 0.98, P2Rank 0.56). Use the 3D pocket comparison to verify whether they identify the same site. Central metabolic position More central than 93.2% of genes in this genome. No isoenzyme backup detected Imported GPR rules do not show an alternative enzyme for the catalyzed reaction set. Review the complete evidence below

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: Hit
Human identity (%): 28.125 Lower values reduce human off-target concern.
Human E-value: 3.1900000000000003e-32
Gut microbiome similarity: 0.8% 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.

Localization

Localization: Periplasmic

Structure confidence

ColabFold pLDDT: 95.39 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 0.985

Structure A0A0H3GMJ1

Pocket Pocket 15

P2Rank 0.565

Structure A0A0H3GMJ1

Pocket Pocket 1

ColabFold model

FPocket 0.875 · Pocket 19

P2Rank 0.671 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 38 / 4744 genomes with a hit

Prevalence 0.8%

Cross-references

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

Metabolic context

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

Explore metabolic network

Attractive metabolic target: catalyzes a producing chokepoint reaction in Glycine, serine and threonine metabolism, no isoenzyme backup detected, more central than 93.2% of genes in this genome.

Relative network centrality 93.2% more central than 93.2% of genes in this genome

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MANGLKFSPRKTALALAVAVVCAWQSPAFAHGSEAHMVPLDKTLQEFGADVQWDDYAQMFTLIKDGAYVKVKPGAKTAIVNGKSLDLPVPVVMKEGKAWVSDTFINDVFQSGLDQTFQVEKRPHPLNSLSAAEISEAVTIVKAAPEFQPNTRFTEISLHEPDKAAVWAFALQGTPVDAPRTADVVMLDGKHVIEAVVDLQNKKILSWTPIKGAHGMVLLDDFVSVQNIINTSSEFAEVLKKHGITDPGKVVTTPLTVGFFDGKDGLQQDARLLKVVSYLDTGDGNYWAHPIENLVAVVDLEAKKIIKIEEGPVIPVPMEPRPYDGRDRNAPAVKPLDITEPEGKNYTITGDTIHWQNWDFHLRLNSRVGPILSTVTYNDNGTKRQVMYEGSLGGMIVPYGDPDVGWYFKAYLDSGDYGMGTLTSPIVRGKDAPSNAVLLDETIADYTGKPTTIPGAVAIFERYAGPEYKHLEMGKPNVSTERRELVVRWISTVGNYDYIFDWVFHDNGTIGIDAGATGIEAVKGVLAKTMHDPSAKEDTRYGTLIDHNIVGTTHQHIYNFRLDLDVDGENNTLVAMDPEVKPNTAGGPRTSTMQVNQYTIDSEQKAAQKFDPGTIRLLSNTSKENRMGNPVSYQIIPYAGGTHPAATGAKFAPDEWIYHRLSFMDKQLWVTRYHPTERYPEGKYPNRSAHDTGLGQYAKDDESLTNHDDVVWITTGTTHVARAEEWPIMPTEWAHALLKPWNFFDETPTLGEKKK

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

1.4.3.-

Gene Ontology (GO)

GO:0005507 Binding to a copper (Cu) ion.
GO:0008131 Catalysis of the reaction: a primary methyl amine + H2O + O2 = an aldehyde + H2O2 + NH4+.
GO:0048038 Binding to a quinone, any member of a class of diketones derivable from aromatic compounds by conversion of two CH groups into CO groups with any necessary rearrangement of double bonds.
GO:0009308 The chemical reactions and pathways involving any organic compound that is weakly basic in character and contains an amino or a substituted amino group. Amines are called primary, secondary, or tertiary according to whether one, two, or three carbon atoms are attached to the nitrogen atom.
GO:0042597 The region between the inner (cytoplasmic) and outer membrane (Gram-negative Bacteria) or cytoplasmic membrane and cell wall (Fungi and Gram-positive Bacteria).
GO:0006584 The chemical reactions and pathways involving any of a group of physiologically important biogenic amines that possess a catechol (3,4-dihydroxyphenyl) nucleus and are derivatives of 3,4-dihydroxyphenylethylamine.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

36 records

Show feature table

Start	End	DB	Term	Name
216	317	Pfam	PF02728	Copper amine oxidase, N3 domain
216	317	InterPro	IPR015802	Copper amine oxidase, N3-terminal
124	209	Pfam	PF02727	Copper amine oxidase, N2 domain
124	209	InterPro	IPR015800	Copper amine oxidase, N2-terminal
217	322	Gene3D	G3DSA:3.10.450.40	-
1	30	SignalP_GRAM_NEGATIVE	SignalP-noTM	SignalP-noTM
344	751	Gene3D	G3DSA:2.70.98.20	Copper amine oxidase, catalytic domain
344	751	InterPro	IPR036460	Copper amine oxidase, catalytic domain superfamily
1	30	SignalP_GRAM_POSITIVE	SignalP-TM	SignalP-TM
1	32	Phobius	SIGNAL_PEPTIDE	Signal peptide region
337	750	Pfam	PF01179	Copper amine oxidase, enzyme domain
337	750	InterPro	IPR015798	Copper amine oxidase, catalytic domain
485	498	ProSitePatterns	PS01164	Copper amine oxidase topaquinone signature.
485	498	InterPro	IPR000269	Copper amine oxidase
107	218	FunFam	G3DSA:3.10.450.40:FF:000025	Primary amine oxidase
122	214	SUPERFAMILY	SSF54416	Amine oxidase N-terminal region
122	214	InterPro	IPR016182	Copper amine oxidase, N-terminal
216	325	SUPERFAMILY	SSF54416	Amine oxidase N-terminal region
216	325	InterPro	IPR016182	Copper amine oxidase, N-terminal
714	727	ProSitePatterns	PS01165	Copper amine oxidase copper-binding site signature.
714	727	InterPro	IPR000269	Copper amine oxidase
13	24	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
120	751	PANTHER	PTHR10638	COPPER AMINE OXIDASE
120	751	InterPro	IPR000269	Copper amine oxidase
33	755	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
25	32	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
1	12	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
333	751	SUPERFAMILY	SSF49998	Amine oxidase catalytic domain
333	751	InterPro	IPR036460	Copper amine oxidase, catalytic domain superfamily
36	114	Gene3D	G3DSA:3.30.457.10	-
36	114	InterPro	IPR036582	Copper amine oxidase-like, N-terminal domain superfamily
36	110	Pfam	PF07833	Copper amine oxidase N-terminal domain
36	110	InterPro	IPR012854	Copper amine oxidase-like, N-terminal
116	216	Gene3D	G3DSA:3.10.450.40	-
36	115	SUPERFAMILY	SSF55383	Copper amine oxidase, domain N
36	115	InterPro	IPR036582	Copper amine oxidase-like, N-terminal domain superfamily

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.

Download VMD script Full viewer

Loading 3D structure...

Drag to rotate — click the view, then scroll to zoom.

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 #15

0.985

Show in viewer

Surrounding area

Site 2 FPocket #12

0.46

Show in viewer

Surrounding area

Site 3 FPocket #36

0.31

Show in viewer

Surrounding area

Site 4 FPocket #23

0.23

Show in viewer

Surrounding area

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.565

Show in viewer

Surrounding area

Site 2 P2Rank #2

0.377

Show in viewer

Surrounding area

Site 3 P2Rank #3

0.317

Show in viewer

Surrounding area

Site 4 P2Rank #4

0.223

Show in viewer

Surrounding area

Site 5 P2Rank #5

0.206

Show in viewer

Surrounding area

Residue sets

UniProt: Active site:413-413 Proton acceptor

UniProt: Active site:496-496 Schiff-base intermediate with substrate; via topaquinone

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.671

Show in viewer

Surrounding area

Site 2 P2Rank #2

0.319

Show in viewer

Surrounding area

Site 3 P2Rank #3

0.194

Show in viewer

Surrounding area

Site 4 P2Rank #4

0.148

Show in viewer

Surrounding area

Site 5 P2Rank #5

0.106

Show in viewer

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_A0A0H3GMJ1	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_1043	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.

74 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 24 records from similar proteins

Structural ligands 15 0 loaded crystals

Measured bioactivity 9 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

ABN PDB via homolog 107.2 Da · LogP 1.15 · TPSA 26.0 Open detail RCSB PDB

E9C PDB via homolog Detail RCSB PDB

FOR PDB via homolog Detail RCSB PDB

HDZ PDB via homolog Detail RCSB PDB

HY1 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
ABN RCSB PDB	4EV5	P12807	107.2 Da LogP 1.15 TPSA 26.0	✓ Ro5	✓ Clean	`c1ccc(cc1)CN`
E9C RCSB PDB	6L9C	P46881	211.2 Da LogP -1.17 TPSA 114.5	✓ Ro5	Alert	`C1C(=O)C(=CC(=O)C1=O)C[C@@H](C(=O)O)N`
FOR RCSB PDB	4KFE	P12807	30.0 Da LogP -0.18 TPSA 17.1	✓ Ro5	✓ Clean	`C=O`
HDZ RCSB PDB	3WA3	P46881	28.0 Da LogP 0.03 TPSA 47.6	✓ Ro5	✓ Clean	`N#N`
HY1 RCSB PDB	1D6U	P46883	120.2 Da LogP 1.43 TPSA 17.1	✓ Ro5	✓ Clean	`c1ccc(cc1)CC=O`
NEH RCSB PDB	4EV2	P12807	45.1 Da LogP -0.03 TPSA 26.0	✓ Ro5	✓ Clean	`CCN`
OXY RCSB PDB	3WA2	P46881	32.0 Da LogP 0.07 TPSA 34.1	✓ Ro5	✓ Clean	`O=O`
PEA RCSB PDB	1D6U	P46883	122.2 Da LogP 0.47 TPSA 27.6	✓ Ro5	✓ Clean	`c1ccc(cc1)CC[NH3+]`
PEL RCSB PDB	3X3X	P46881	122.2 Da LogP 1.22 TPSA 20.2	✓ Ro5	✓ Clean	`c1ccc(cc1)CCO`
PEO RCSB PDB	4EV5	P12807	34.0 Da LogP 0.02 TPSA 40.5	✓ Ro5	✓ Clean	`OO`
R4A RCSB PDB	2CFD	P46881	805.1 Da LogP 7.65 TPSA 31.9	2 viol.	✓ Clean	`CN(C)c1cccc(c1)OCCCCC2=CCN3C4=C5C(=CC=CN5[Ru]36…`
R5A RCSB PDB	2CFK	P46881	817.1 Da LogP 6.94 TPSA 31.9	2 viol.	✓ Clean	`CN(C)c1cccc(c1)OCCCCCC2=C3C=CC4=CC=CN5C4=C3N([R…`
R7U RCSB PDB	2CFW	P46881	845.2 Da LogP 7.72 TPSA 31.9	2 viol.	✓ Clean	`CN(C)c1cccc(c1)OCCCCCCCC2=C3C=CC4=CC=CN5C4=C3N(…`
R9A RCSB PDB	2CG0	P46881	873.2 Da LogP 8.50 TPSA 31.9	2 viol.	✓ Clean	`CN(C)c1cccc(c1)OCCCCCCCCCC2=C3C=CC4=CC=CN5C4=C3…`
XE RCSB PDB	2W0Q	P46883	131.3 Da LogP 0.00 TPSA 0.0	✓ Ro5	✓ Clean	`[Xe]`

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
CHEMBL1089 ChEMBL	Q16853	7.70 ~20.0 nM	136.2 Da LogP 0.69 TPSA 38.0	✓ Ro5	✓ Clean	`NNCCc1ccccc1`
CHEMBL1240877 ChEMBL	Q16853	6.96 ~109.6 nM	150.2 Da LogP 1.03 TPSA 29.3	✓ Ro5	✓ Clean	`CN(N)CCc1ccccc1`
CHEMBL3919913 ChEMBL	Q16853	6.75 ~177.8 nM	276.8 Da LogP 2.35 TPSA 55.1	✓ Ro5	✓ Clean	`Cl.NCC(=O)NCc1cccc(-c2ccccc2)c1`
CHEMBL1241003 ChEMBL	Q16853	6.74 ~182.0 nM	164.3 Da LogP 1.42 TPSA 29.3	✓ Ro5	✓ Clean	`CCN(N)CCc1ccccc1`
CHEMBL1241069 ChEMBL	Q16853	6.62 ~239.9 nM	164.3 Da LogP 1.42 TPSA 29.3	✓ Ro5	✓ Clean	`CN(N)CCCc1ccccc1`
CHEMBL1241379 ChEMBL	Q16853	6.57 ~269.2 nM	136.2 Da LogP 0.99 TPSA 29.3	✓ Ro5	✓ Clean	`CN(N)Cc1ccccc1`
CHEMBL3990105 ChEMBL	Q9TTK6	6.43 ~371.5 nM	240.3 Da LogP 1.93 TPSA 55.1	✓ Ro5	✓ Clean	`NCC(=O)NCc1cccc(-c2ccccc2)c1`
CHEMBL1241067 ChEMBL	Q16853	6.36 ~436.5 nM	192.3 Da LogP 2.06 TPSA 29.3	✓ Ro5	✓ Clean	`CC(C)CN(N)CCc1ccccc1`
CHEMBL3961247 ChEMBL	Q9TTK6	6.30 ~501.2 nM	173.3 Da LogP 2.29 TPSA 26.0	✓ Ro5	✓ Clean	`NCC=C=CCCc1ccccc1`

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
ZINC38072395 ZINC	0.684	259.4 Da LogP 4.48 TPSA 26.0	✓ Ro5	✓ Clean	`NCc1ccc(-c2ccc(-c3ccccc3)cc2)cc1`
ZINC42419086 ZINC	0.649	243.1 Da LogP 1.02 TPSA 55.1	✓ Ro5	✓ Clean	`NCC(=O)NCc1cccc(Br)c1`
ZINC37870845 ZINC	0.639	221.3 Da LogP -0.62 TPSA 84.2	✓ Ro5	✓ Clean	`NCC(=O)NCC(=O)NCc1ccccc1`
ZINC20357643 ZINC	0.625	212.2 Da LogP 3.22 TPSA 26.3	✓ Ro5	✓ Clean	`O=CCc1ccc(Oc2ccccc2)cc1`
ZINC52943184 ZINC	0.625	209.2 Da LogP 0.17 TPSA 98.3	✓ Ro5	✓ Clean	`NCC(=O)NCc1cccc([N+](=O)[O-])c1`
ZINC34544406 ZINC	0.615	226.3 Da LogP 3.01 TPSA 26.3	✓ Ro5	✓ Clean	`O=CCc1ccc(OCc2ccccc2)cc1`
ZINC2382315901 ZINC	0.613	270.4 Da LogP 1.85 TPSA 62.1	✓ Ro5	✓ Clean	`NNCCc1ccccc1NNCCc1ccccc1`
ZINC19269027 ZINC	0.600	215.1 Da LogP 1.45 TPSA 38.0	✓ Ro5	✓ Clean	`NNCCc1ccc(Br)cc1`
ZINC19486498 ZINC	0.600	232.2 Da LogP 1.28 TPSA 55.1	✓ Ro5	✓ Clean	`NCC(=O)NCc1cccc(C(F)(F)F)c1`
ZINC409791 ZINC	0.600	284.4 Da LogP 2.93 TPSA 40.5	✓ Ro5	✓ Clean	`OCCc1ccc(CCCc2ccc(CCO)cc2)cc1`
ZINC5114045 ZINC	0.600	211.2 Da LogP -0.69 TPSA 117.7	✓ Ro5	Alert	`N[C@@H](CC1=CC(=O)C(=O)C=C1O)C(=O)O`
ZINC694778 ZINC	0.600	372.5 Da LogP 3.40 TPSA 58.2	✓ Ro5	✓ Clean	`O=C(Cc1ccccc1)NCc1cccc(CNC(=O)Cc2ccccc2)c1`
ZINC35719996 ZINC	0.591	215.3 Da LogP 3.30 TPSA 26.0	✓ Ro5	✓ Clean	`NCc1ccc(Sc2ccccc2)cc1`
ZINC90624709 ZINC	0.585	317.4 Da LogP 3.92 TPSA 49.3	✓ Ro5	✓ Clean	`O=C(Cc1ccc(-c2ccccc2)cc1)NCc1cccc(O)c1`
ZINC19261613 ZINC	0.583	227.3 Da LogP 2.86 TPSA 35.2	✓ Ro5	✓ Clean	`NCc1cccc(COCc2ccccc2)c1`
ZINC2524597 ZINC	0.583	213.3 Da LogP 2.72 TPSA 35.2	✓ Ro5	✓ Clean	`NCc1ccc(OCc2ccccc2)cc1`
ZINC88243073 ZINC	0.583	234.4 Da LogP 2.53 TPSA 29.3	✓ Ro5	✓ Clean	`CC(C)C[C@H](N)CN(C)CCc1ccccc1`
ZINC88243074 ZINC	0.583	234.4 Da LogP 2.53 TPSA 29.3	✓ Ro5	✓ Clean	`CC(C)C[C@@H](N)CN(C)CCc1ccccc1`
ZINC1875373373 ZINC	0.571	253.3 Da LogP 2.37 TPSA 41.6	✓ Ro5	✓ Clean	`O=C(NCc1cccc(-c2ccccc2)c1)[C@@H]1CO1`
ZINC1875373374 ZINC	0.571	253.3 Da LogP 2.37 TPSA 41.6	✓ Ro5	✓ Clean	`O=C(NCc1cccc(-c2ccccc2)c1)[C@H]1CO1`
ZINC32581997 ZINC	0.571	240.3 Da LogP 2.77 TPSA 42.0	✓ Ro5	✓ Clean	`CCC(=O)NCc1cccc(-c2ccncc2)c1`
ZINC50040300 ZINC	0.571	215.1 Da LogP 1.45 TPSA 38.0	✓ Ro5	✓ Clean	`NNCCc1cccc(Br)c1`
ZINC83852840 ZINC	0.571	220.4 Da LogP 2.14 TPSA 29.3	✓ Ro5	✓ Clean	`CC(C)[C@H](N)CN(C)CCc1ccccc1`
ZINC83852841 ZINC	0.571	220.4 Da LogP 2.14 TPSA 29.3	✓ Ro5	✓ Clean	`CC(C)[C@@H](N)CN(C)CCc1ccccc1`
ZINC3438522 ZINC	0.568	301.4 Da LogP 4.21 TPSA 29.1	✓ Ro5	✓ Clean	`O=C(Cc1ccc(-c2ccccc2)cc1)NCc1ccccc1`
ZINC97757833 ZINC	0.565	294.4 Da LogP 2.97 TPSA 41.1	✓ Ro5	✓ Clean	`O=C(C[C@@H]1CCNC1)NCc1cccc(-c2ccccc2)c1`
ZINC97757834 ZINC	0.565	294.4 Da LogP 2.97 TPSA 41.1	✓ Ro5	✓ Clean	`O=C(C[C@H]1CCNC1)NCc1cccc(-c2ccccc2)c1`
ZINC77325824 ZINC	0.561	316.4 Da LogP 3.74 TPSA 55.1	✓ Ro5	✓ Clean	`NC(=O)c1cccc(CNCc2cccc(-c3ccccc3)c2)c1`
ZINC1574115 ZINC	0.556	226.3 Da LogP 2.19 TPSA 52.0	✓ Ro5	✓ Clean	`NCc1ccc(Cc2ccc(CN)cc2)cc1`
ZINC34189702 ZINC	0.556	214.3 Da LogP 3.01 TPSA 29.5	✓ Ro5	✓ Clean	`OCCc1cccc(Oc2ccccc2)c1`
ZINC43875619 ZINC	0.556	212.2 Da LogP 3.22 TPSA 26.3	✓ Ro5	✓ Clean	`O=CCc1cccc(Oc2ccccc2)c1`
ZINC5763419 ZINC	0.556	212.3 Da LogP 2.27 TPSA 52.0	✓ Ro5	✓ Clean	`NCc1ccc(-c2ccc(CN)cc2)cc1`
ZINC91755660 ZINC	0.553	323.4 Da LogP 1.52 TPSA 78.5	✓ Ro5	✓ Clean	`O=C(CN1C(=O)CNC1=O)NCc1cccc(-c2ccccc2)c1`
ZINC1164584 ZINC	0.553	400.5 Da LogP 4.18 TPSA 58.2	✓ Ro5	✓ Clean	`O=C(CCc1ccccc1)NCc1cccc(CNC(=O)CCc2ccccc2)c1`
ZINC1176481 ZINC	0.550	404.5 Da LogP 3.08 TPSA 76.7	✓ Ro5	✓ Clean	`O=C(COc1ccccc1)NCc1cccc(CNC(=O)COc2ccccc2)c1`
ZINC2836318 ZINC	0.550	436.6 Da LogP 4.50 TPSA 58.2	✓ Ro5	✓ Clean	`O=C(CSc1ccccc1)NCc1cccc(CNC(=O)CSc2ccccc2)c1`
ZINC167004 ZINC	0.545	201.1 Da LogP 1.98 TPSA 20.2	✓ Ro5	✓ Clean	`OCCc1ccc(Br)cc1`
ZINC19633944 ZINC	0.545	234.4 Da LogP 2.50 TPSA 6.5	✓ Ro5	✓ Clean	`CCN(CCCc1ccccc1)CCN(C)C`
ZINC33756134 ZINC	0.545	248.1 Da LogP 1.83 TPSA 20.2	✓ Ro5	✓ Clean	`OCCc1ccc(I)cc1`
ZINC388032 ZINC	0.545	233.1 Da LogP 1.75 TPSA 26.0	✓ Ro5	✓ Clean	`NCc1cccc(I)c1`
ZINC40448470 ZINC	0.545	246.0 Da LogP 2.03 TPSA 17.1	✓ Ro5	✓ Clean	`O=CCc1ccc(I)cc1`
ZINC46087423 ZINC	0.545	207.3 Da LogP 2.20 TPSA 12.5	✓ Ro5	✓ Clean	`COCCN(C)CCCc1ccccc1`
ZINC89678026 ZINC	0.545	297.4 Da LogP 1.95 TPSA 84.2	✓ Ro5	✓ Clean	`Cc1cccc(-c2cccc(CNC(=O)CNC(N)=O)c2)c1`
ZINC97551288 ZINC	0.543	295.4 Da LogP 3.40 TPSA 38.3	✓ Ro5	✓ Clean	`COCC1(C(=O)NCc2cccc(-c3ccccc3)c2)CC1`
ZINC169621139 ZINC	0.543	297.4 Da LogP 2.65 TPSA 67.2	✓ Ro5	✓ Clean	`NNCCc1ccc(NC(=O)CCCc2ccccc2)cc1`
ZINC11945494 ZINC	0.542	213.3 Da LogP 2.72 TPSA 35.2	✓ Ro5	✓ Clean	`NCc1ccc(COc2ccccc2)cc1`
ZINC1494952 ZINC	0.542	211.3 Da LogP 2.38 TPSA 43.1	✓ Ro5	✓ Clean	`NCc1ccc(C(=O)c2ccccc2)cc1`
ZINC82048495 ZINC	0.542	247.3 Da LogP 1.98 TPSA 60.2	✓ Ro5	✓ Clean	`NCc1ccc(S(=O)(=O)c2ccccc2)cc1`
ZINC88243046 ZINC	0.541	234.4 Da LogP 2.53 TPSA 29.3	✓ Ro5	✓ Clean	`CC[C@H](C)[C@H](N)CN(C)CCc1ccccc1`
ZINC88243048 ZINC	0.541	234.4 Da LogP 2.53 TPSA 29.3	✓ Ro5	✓ Clean	`CC[C@H](C)[C@@H](N)CN(C)CCc1ccccc1`

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.

VK055_1043

Strong target candidate with converging metabolic, structural and chemical evidence.

Main supporting evidence

Risks to review

Evidence coverage

Prioritization evidence

Off-target risk

Essentiality

Localization

Structure confidence

Binding-site evidence

Cross-references

Sequence

Chemistry

Pathways

Metabolic context

Sequence

Functional annotations

Enzyme Commission (EC)

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · FPocket

Binding pockets · P2Rank

Binding pockets · FPocket

Binding pockets · P2Rank

Structural evidence

Ligand evidence