KpKP13 Protein target profile

DNA gyrase subunit A

Accession: KP13_00955

Gene: gyrA AHE43517.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3H0Y6

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Length 877

Pocket druggability (P2Rank · AlphaFold DB model) 0.754

Direct ligand evidence 0 91 total records

Functional annotation 1 EC 11 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

Second pocket predictor agrees P2Rank predicted binding-site probability 0.75. Structure available AlphaFold DB model + ColabFold model Ligand evidence via structure/bioactivity 25 structural and 16 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 (%): 27.566 Lower values reduce human off-target concern.
Human E-value: 1.59e-15
Gut microbiome similarity: 8.5% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 95.886 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 86.72 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) 0.754

Structure A0A0H3H0Y6

Pocket Pocket 1

Druggability (FPocket) 0.336

Structure A0A0H3H0Y6

Pocket Pocket 50

ColabFold model

P2Rank 0.79 · Pocket 1

FPocket 0.665 · Pocket 10

Core conservation Accessory gene

Roary accessory

CoreCruncher accessory

Gut microbiome 404 / 4744 genomes with a hit

Prevalence 8.5%

Sequence

Primary amino-acid sequence viewer.

MSDLAREITPVNIEEELKNSYLDYAMSVIVGRALPDVRDGLKPVHRRVLYAMNVLGNDWNKAYKKSARVVGDVIGKYHPHGDFAVYNTIVRMAQPFSLRYMLVDGQGNFGSIDGDSAAAMRYTEIRLAKIAHELMADLEKETVDFVDNYDGTERIPDVMPTKIPNLLVNGASGIAVGMATNIPPHNLTEVINGCLAYVDDEDISIEGLMAHIPGPDFPTAAIINGRRGIEEAYRTGRGKVYIRARAEVEVDAKSGRETIIVHEIPYQVNKARLIEKIAELVKEKRVEGISALRDESDKDGMRIVIEVKRDAVGEVVLNNLYSQTQLQVSFGINMVALHHGQPKIMNLKDIIAAFVRHRREVVTRRTIFELRKARDRAHILEALAVALANIDPIIELIRRAPTPAEAKTALVAQAWDLGNVAAMLERAGDDAARPEWLEPEFGVRDGKYYLTEQQAQAILDLRLQKLTGLEHEKLLDEYKELLEQIAELLHILGSADRLMEVIREELELIRDQFGDERRTEITANSADINIEDLINQEDVVVTLSHQGYVKYQPLTDYEAQRRGGKGKSAARIKEEDFIDRLLVANTHDTILCFSSRGRLYWMKVYQLPEASRGARGRPIVNLLPLEADERITAILPVREYEEGVNVFMATASGTVKKTALTEFSRPRSAGIIAVNLNEGDELIGVDLTSGQDEVMLFSAAGKVVRFKEDAVRAMGRTATGVRGIKLAENDSVVSLIIPRGEGAILTVTQNGYGKRTAAAEYPTKSRATQGVISIKVTERNGSVVGAVQVDDCDQIMMITDAGTLVRTRVSEVSIVGRNTQGVILIRTAEDENVVGLQRVAEPVDDEELDAIDGSAAEGDDDIAPEADTDDDIAEDEE

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 11 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

5.6.2.2

Gene Ontology (GO)

GO:0006265 The process in which a transformation is induced in the topological structure of a double-stranded DNA helix, resulting in a change in linking number.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0003916 Catalysis of the transient cleavage and passage of individual DNA strands or double helices through one another, resulting a topological transformation in double-stranded DNA.
GO:0006259 Any cellular metabolic process involving deoxyribonucleic acid. This is one of the two main types of nucleic acid, consisting of a long, unbranched macromolecule formed from one, or more commonly, two, strands of linked deoxyribonucleotides.
GO:0003918 Catalysis of a DNA topological transformation by transiently cleaving a pair of complementary DNA strands to form a gate through which a second double-stranded DNA segment is passed, after which the severed strands in the first DNA segment are rejoined, driven by ATP hydrolysis. The enzyme changes the linking number in multiples of 2.
GO:0005694 A structure composed of a very long molecule of DNA and associated proteins (e.g. histones) that carries hereditary information.
GO:0003677 Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0009330 Complex that possesses DNA topoisomerase II (double strand cut, ATP-hydrolyzing) activity.
GO:0034335 Catalytic introduction of negative supercoils into a DNA molecule or region thereof. In bacteria, negative supercoils are only introduced by DNA gyrase, a type II topoisomerase, but not all DNA gyrases are capable of introducing supercoils. In bacteria, the level of supercoiling varies widely between species and has been characterized properly in only a handful of organisms. The best characterized enzyme, from E.coli, is exceptionally proficient at supercoiling and this ability is not representative of all bacteria.
GO:0006261 A DNA replication process that uses parental DNA as a template for the DNA-dependent DNA polymerases that synthesize the new strands.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

39 records

Show feature table

Start	End	DB	Term	Name
32	279	FunFam	G3DSA:3.90.199.10:FF:000001	DNA gyrase subunit A
1	841	Hamap	MF_01897	DNA gyrase subunit A [gyrA].
1	841	InterPro	IPR005743	DNA gyrase, subunit A
32	521	Gene3D	G3DSA:3.90.199.10	Topoisomerase II, domain 5
32	521	InterPro	IPR013758	DNA topoisomerase, type IIA, domain A, alpha-beta
531	840	FunFam	G3DSA:2.120.10.90:FF:000002	DNA gyrase subunit A
471	491	Coils	Coil	Coil
30	507	CDD	cd00187	TOP4c
30	507	InterPro	IPR002205	DNA topoisomerase, type IIA, domain A
8	840	NCBIfam	TIGR01063	DNA gyrase subunit A
236	333	Gene3D	G3DSA:3.30.1360.40	-
5	845	PANTHER	PTHR43493	DNA GYRASE/TOPOISOMERASE SUBUNIT A
538	584	Pfam	PF03989	DNA gyrase C-terminal domain, beta-propeller
538	584	InterPro	IPR006691	DNA gyrase/topoisomerase IV, subunit A, C-terminal repeat
793	839	Pfam	PF03989	DNA gyrase C-terminal domain, beta-propeller
793	839	InterPro	IPR006691	DNA gyrase/topoisomerase IV, subunit A, C-terminal repeat
744	789	Pfam	PF03989	DNA gyrase C-terminal domain, beta-propeller
744	789	InterPro	IPR006691	DNA gyrase/topoisomerase IV, subunit A, C-terminal repeat
645	688	Pfam	PF03989	DNA gyrase C-terminal domain, beta-propeller
645	688	InterPro	IPR006691	DNA gyrase/topoisomerase IV, subunit A, C-terminal repeat
588	637	Pfam	PF03989	DNA gyrase C-terminal domain, beta-propeller
588	637	InterPro	IPR006691	DNA gyrase/topoisomerase IV, subunit A, C-terminal repeat
692	737	Pfam	PF03989	DNA gyrase C-terminal domain, beta-propeller
692	737	InterPro	IPR006691	DNA gyrase/topoisomerase IV, subunit A, C-terminal repeat
236	333	FunFam	G3DSA:3.30.1360.40:FF:000002	DNA gyrase subunit A
370	492	Gene3D	G3DSA:1.10.268.10	Topoisomerase, domain 3
370	492	InterPro	IPR013757	DNA topoisomerase, type IIA, alpha-helical domain superfamily
845	877	MobiDBLite	mobidb-lite	consensus disorder prediction
32	506	Pfam	PF00521	DNA gyrase/topoisomerase IV, subunit A
32	506	InterPro	IPR002205	DNA topoisomerase, type IIA, domain A
839	877	MobiDBLite	mobidb-lite	consensus disorder prediction
531	840	Gene3D	G3DSA:2.120.10.90	-
531	840	InterPro	IPR035516	DNA gyrase/topoisomerase IV, subunit A, C-terminal
30	521	SUPERFAMILY	SSF56719	Type II DNA topoisomerase
30	521	InterPro	IPR013760	DNA topoisomerase, type IIA-like domain superfamily
11	499	SMART	SM00434	topIV4
11	499	InterPro	IPR002205	DNA topoisomerase, type IIA, domain A
533	851	SUPERFAMILY	SSF101904	GyrA/ParC C-terminal domain-like
533	851	InterPro	IPR035516	DNA gyrase/topoisomerase IV, subunit A, C-terminal

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

0.754

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Surrounding area

Pocket 2 P2Rank #2

0.192

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Surrounding area

Pocket 3 P2Rank #3

0.038

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Surrounding area

Pocket 4 P2Rank #4

0.032

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Surrounding area

Pocket 5 P2Rank #5

0.02

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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 #50

0.336

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Surrounding area

Pocket 2 FPocket #40

0.211

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Surrounding area

Residue sets

UniProt: Active site:122-122 O-(5'-phospho-DNA)-tyrosine intermediate

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.79

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Surrounding area

Pocket 2 P2Rank #2

0.07

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Surrounding area

Pocket 3 P2Rank #3

0.049

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Surrounding area

Pocket 4 P2Rank #4

0.041

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Surrounding area

Pocket 5 P2Rank #5

0.022

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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 #10

0.665

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Surrounding area

Pocket 2 FPocket #34

0.35

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Surrounding area

Pocket 3 FPocket #51

0.228

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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_A0A0H3H0Y6	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_00955	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.

91 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 41 records from similar proteins

Structural ligands 25 0 loaded crystals

Measured bioactivity 16 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

31N PDB via homolog 509.5 Da · LogP 2.28 · TPSA 127.7 Open detail RCSB PDB

50M PDB via homolog Detail RCSB PDB

6EJ PDB via homolog Detail RCSB PDB

8MX PDB via homolog Detail RCSB PDB

94H 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
31N RCSB PDB	4PLB	P20831	509.5 Da LogP 2.28 TPSA 127.7	1 viol.	✓ Clean	`COc1ccc2c(n1)c(c(cn2)F)C[C@@H](C34CCC(CC3)(CO4)…`
50M RCSB PDB	5CDO	Q99XG5	374.4 Da LogP 1.33 TPSA 134.4	✓ Ro5	✓ Clean	`C[C@@H]1CN2c3ccc(cc3C[C@]4([C@H]2[C@@H](O1)C)C(…`
6EJ RCSB PDB	5IWI	Q99XG5	451.5 Da LogP 2.05 TPSA 81.5	✓ Ro5	✓ Clean	`c1cc(c2c3c1C=CC(=O)N3C[C@H]2CN4CCC(CC4)NCc5cc6c…`
8MX RCSB PDB	5BTL	P9WG47	385.4 Da LogP 2.67 TPSA 74.6	✓ Ro5	✓ Clean	`Cc1c2c(cc(c1N3C[C@@H]4CCCN[C@@H]4C3)F)C(=O)C(=C…`
94H RCSB PDB	5NPK	Q99XG5	362.5 Da LogP 3.72 TPSA 83.8	✓ Ro5	✓ Clean	`c1ccc(cc1)[C@H](CN)NC(=O)c2cc(cs2)c3c[nH]c4c3cc…`
94K RCSB PDB	5NPP	Q99XG5	370.9 Da LogP 4.81 TPSA 55.1	✓ Ro5	✓ Clean	`Cc1c(cc(s1)c2ccccc2Cl)C(=O)N[C@@H](CN)c3ccccc3`
9JN RCSB PDB	5NPK	Q99XG5	362.5 Da LogP 3.72 TPSA 83.8	✓ Ro5	✓ Clean	`c1ccc(cc1)[C@@H](CN)NC(=O)c2cc(cs2)c3c[nH]c4c3c…`
AE8 RCSB PDB	4BUL	Q99XG5	467.5 Da LogP 1.16 TPSA 101.7	✓ Ro5	✓ Clean	`c1c(ncc2c1OCCO2)CNC3CCN(CC3)C[C@@]4(CN5c6c4c(cn…`
ANP RCSB PDB	6RKW	P0AES4	506.2 Da LogP -2.06 TPSA 281.9	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
DG RCSB PDB	6QX2	Q99XG5	347.2 Da LogP -1.54 TPSA 185.8	✓ Ro5	✓ Clean	`c1nc2c(n1[C@H]3C[C@@H]([C@H](O3)COP(=O)(O)O)O)N…`
DT RCSB PDB	5CDM	Q99XG5	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`CC1=CN(C(=O)NC1=O)[C@H]2C[C@@H]([C@H](O2)COP(=O…`
DU5 RCSB PDB	6FM4	Q99XG5	374.5 Da LogP 3.18 TPSA 48.5	✓ Ro5	✓ Clean	`c1ccc(cc1)C(=O)NCCCN2CCN(CC2)c3c4ccccc4ccn3`
E32 RCSB PDB	6FQM	Q99XG5	327.4 Da LogP 1.66 TPSA 68.6	✓ Ro5	✓ Clean	`c1cn-2c(n1)C(=O)N(c3c2cc(c(c3)N4CC[C@@H](C4)N)F…`
E3E RCSB PDB	6FQS	Q99XG5	320.3 Da LogP 3.19 TPSA 52.2	✓ Ro5	✓ Clean	`c1cnccc1c2cc3c(cc2F)-n4ccnc4C(=O)N3C5CC5`
EVP RCSB PDB	5CDN	Q99XG5	588.6 Da LogP 1.34 TPSA 160.8	2 viol.	✓ Clean	`C[C@@H]1OC[C@@H]2[C@@H](O1)[C@@H]([C@H]([C@@H](…`
GFN RCSB PDB	5BTD	P9WG47	375.4 Da LogP 1.98 TPSA 83.8	✓ Ro5	✓ Clean	`C[C@H]1CN(CCN1)c2c(cc3c(c2OC)N(C=C(C3=O)C(=O)O)…`
JHN RCSB PDB	6RKS	P0AES4	448.5 Da LogP 1.09 TPSA 94.3	✓ Ro5	✓ Clean	`c1c2c(cnc1CNC3CCN(CC3)C[C@@H]4CN5C(=O)C=CC6=C5N…`
JK8 RCSB PDB	6QX1	Q99XG5	364.8 Da LogP 5.23 TPSA 61.3	1 viol.	✓ Clean	`c1ccc(cc1)[C@H](CN)Oc2c3cc(ccc3on2)c4ccccc4Cl`
LFX RCSB PDB	4Z2D	Q8DPM2	361.4 Da LogP 1.54 TPSA 75.0	✓ Ro5	✓ Clean	`C[C@H]1COc2c3c(cc(c2N4CCN(CC4)C)F)C(=O)C(=CN31)…`
MFX RCSB PDB	4Z2C	Q8DPM2	401.4 Da LogP 2.37 TPSA 83.8	✓ Ro5	✓ Clean	`COc1c2c(cc(c1N3C[C@@H]4CCCN[C@@H]4C3)F)C(=O)C(=…`
Q52 RCSB PDB	6Z1A	P20831	410.9 Da LogP 4.09 TPSA 50.3	✓ Ro5	✓ Clean	`COc1ccc2c(n1)c(ccn2)CCN3CCC(CC3)NCc4ccc(cc4)Cl`
RXV RCSB PDB	2XCR	Q99XG5	461.6 Da LogP 3.75 TPSA 83.3	✓ Ro5	✓ Clean	`COc1ccc2c(c1)c(c(cn2)C#N)CCN3CCC(CC3)NCc4cc5c(c…`
SM8 RCSB PDB	2Y3P	P0AES5	932.3 Da LogP 3.00 TPSA 309.4	3 viol.	✓ Clean	`C[C@@H]1[C@H]([C@@H](C[C@@H](O1)c2ccc3c(c2O)[C@…`
TR6 RCSB PDB	4Z2E	Q8DPM2	416.4 Da LogP 1.89 TPSA 101.5	✓ Ro5	✓ Clean	`c1cc(c(cc1F)F)N2C=C(C(=O)c3c2nc(c(c3)F)N4C[C@@H…`
WCP RCSB PDB	5BS3	P20831	507.5 Da LogP 1.72 TPSA 127.6	1 viol.	✓ Clean	`c1cc2c(nc1CNC34CCC(CC3)(OC4)C[C@@]5(CN6c7c5c(cn…`

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
CHEMBL2424893 ChEMBL	P20831	8.10 ~7.9 nM	478.6 Da LogP 3.36 TPSA 118.1	✓ Ro5	✓ Clean	`COc1ccc2nccc(NC(=O)[C@H]3CC[C@H](NCc4ccc5c(n4)N…`
CHEMBL2165064 ChEMBL	P20831	7.52 ~30.2 nM	463.5 Da LogP 2.24 TPSA 92.4	✓ Ro5	✓ Clean	`N#Cc1ccc2ccc(=O)n(CCN3CC[C@H](NCc4cc5c(cn4)OCCO…`
CHEMBL2424894 ChEMBL	P20831	7.52 ~30.2 nM	450.5 Da LogP 2.66 TPSA 68.6	✓ Ro5	✓ Clean	`O=c1ccc2ccc(F)c3c2n1CC3CN1CCC(NCc2cc3c(cn2)OCCO…`
CHEMBL1276635 ChEMBL	P0AES4	6.92 ~120.2 nM	374.4 Da LogP 3.42 TPSA 71.8	✓ Ro5	✓ Clean	`CC[C@@H]1CCN(c2c(F)cc3c(=O)c(C(=O)O)cn(C4CC4)c3…`
CHEMBL3702487 ChEMBL	P0AES4	6.68 ~208.9 nM	503.9 Da LogP 1.72 TPSA 143.3	1 viol.	✓ Clean	`C[C@@H]1CN(c2noc3c(Cl)c4c(cc23)CC2(C(=O)NC(=O)N…`
CHEMBL430 ChEMBL	P0C1U9	6.52 ~302.0 nM	389.4 Da LogP 0.97 TPSA 123.0	✓ Ro5	✓ Clean	`CO/N=C1\CN(c2nc3c(cc2F)c(=O)c(C(=O)O)cn3C2CC2)C…`
CHEMBL4530328 ChEMBL	P0C1U9	6.52 ~302.0 nM	449.5 Da LogP 2.47 TPSA 94.7	✓ Ro5	✓ Clean	`O=c1nc(NC[C@@H](O)CN2CCN(c3nccc4ccc(F)cc34)CC2)…`
CHEMBL202864 ChEMBL	P0C1U9	6.30 ~501.2 nM	360.4 Da LogP 1.79 TPSA 70.1	✓ Ro5	✓ Clean	`O=c1[nH]sc2c1c(=O)c1cc(F)c(N3CCNCC3)cc1n2C1CC1`
CHEMBL203557 ChEMBL	P0C1U9	6.30 ~501.2 nM	353.4 Da LogP 3.44 TPSA 67.8	✓ Ro5	✓ Clean	`O=c1[nH]sc2c1c(=O)c1cc(F)c(-c3cccnc3)cc1n2C1CC1`
CHEMBL4531900 ChEMBL	P0AES4	6.30 ~501.2 nM	414.5 Da LogP 3.97 TPSA 61.6	✓ Ro5	✓ Clean	`O=c1cc(NCCCN2CCN(c3nccc4ccccc34)CC2)c2ccccc2o1`
CHEMBL4567626 ChEMBL	P0AES4	6.22 ~602.6 nM	449.0 Da LogP 4.62 TPSA 61.6	✓ Ro5	✓ Clean	`O=c1cc(NCCCN2CCN(c3nccc4ccccc34)CC2)c2cc(Cl)ccc…`
CHEMBL4438807 ChEMBL	P20831	6.10 ~794.3 nM	447.5 Da LogP 3.60 TPSA 69.8	✓ Ro5	✓ Clean	`O=c1cc(CC(O)CCN2CCN(c3nccc4ccc(F)cc34)CC2)c2ccc…`
CHEMBL4445613 ChEMBL	P0AES4	6.10 ~794.3 nM	432.5 Da LogP 4.10 TPSA 61.6	✓ Ro5	✓ Clean	`O=c1cc(NCCCN2CCN(c3nccc4ccc(F)cc34)CC2)c2ccccc2…`
CHEMBL4537564 ChEMBL	P0AES4	6.05 ~891.3 nM	432.5 Da LogP 4.10 TPSA 61.6	✓ Ro5	✓ Clean	`O=c1cc(NCCCN2CCN(c3nc(F)cc4ccccc34)CC2)c2ccccc2…`
CHEMBL4570423 ChEMBL	P0AES4	6.05 ~891.3 nM	449.0 Da LogP 4.62 TPSA 61.6	✓ Ro5	✓ Clean	`O=c1cc(NCCCN2CCN(c3nccc4ccc(Cl)cc34)CC2)c2ccccc…`
CPF ChEMBL	P0AES4	6.00 ~1.0 µM	331.3 Da LogP 1.58 TPSA 74.6	✓ Ro5	✓ Clean	`c1c2c(cc(c1F)N3CCNCC3)N(C=C(C2=O)C(=O)O)C4CC4`

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
ZINC13523519 ZINC	1.000	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@@H](O)[C@@H](COP(=O)(O)O)O2)c(…`
ZINC138562667 ZINC	1.000	448.5 Da LogP 1.09 TPSA 94.3	✓ Ro5	✓ Clean	`O=c1ccc2ncc(=O)n3c2n1C[C@H]3CN1CCC(NCc2cc3c(cn2…`
ZINC1532628 ZINC	1.000	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@@H](O)[C@H](COP(=O)(O)O)O2)c(=…`
ZINC1678872 ZINC	1.000	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](O)[C@@H](COP(=O)(O)O)O2)c(=O…`
ZINC20220 ZINC	1.000	331.3 Da LogP 1.58 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)c1cn(C2CC2)c2cc(N3CCNCC3)c(F)cc2c1=O`
ZINC2047010 ZINC	1.000	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@@H](O)[C@H](COP(=O)(O)O)O2)c(=O…`
ZINC223227887 ZINC	1.000	448.5 Da LogP 1.09 TPSA 94.3	✓ Ro5	✓ Clean	`O=c1ccc2ncc(=O)n3c2n1C[C@@H]3CN1CCC(NCc2cc3c(cn…`
ZINC3870253 ZINC	1.000	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@H](COP(=O)(O)O)O2)c(=O…`
ZINC3870254 ZINC	1.000	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](O)[C@H](COP(=O)(O)O)O2)c(=O)…`
ZINC6523446 ZINC	1.000	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@@H](COP(=O)(O)O)O2)c(=…`
ZINC12503053 ZINC	0.837	402.2 Da LogP -1.28 TPSA 197.6	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC33979243 ZINC	0.837	402.2 Da LogP -1.28 TPSA 197.6	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC33979244 ZINC	0.837	402.2 Da LogP -1.28 TPSA 197.6	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)OP(=O)…`
ZINC33979245 ZINC	0.837	402.2 Da LogP -1.28 TPSA 197.6	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@@H](O)[C@H](CO[P@@](=O)(O)OP(=…`
ZINC33979246 ZINC	0.837	402.2 Da LogP -1.28 TPSA 197.6	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@@H](O)[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC8215882 ZINC	0.837	402.2 Da LogP -1.28 TPSA 197.6	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](O)[C@@H](CO[P@@](=O)(O)OP(=O…`
ZINC17107637 ZINC	0.833	320.2 Da LogP -1.46 TPSA 162.7	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@@H](O)[C@@H](COP(N)(N)=O)O2)c(…`
ZINC17107641 ZINC	0.833	320.2 Da LogP -1.46 TPSA 162.7	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@@H](COP(N)(N)=O)O2)c(=…`
ZINC5493427 ZINC	0.833	320.2 Da LogP -1.46 TPSA 162.7	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@H](COP(N)(N)=O)O2)c(=O…`
ZINC5493430 ZINC	0.833	320.2 Da LogP -1.46 TPSA 162.7	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@@H](O)[C@H](COP(N)(N)=O)O2)c(=…`
ZINC12360002 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12360703 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12503599 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC16546165 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@](=O)(O)OP(=O)(…`
ZINC31977053 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC4806433 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC53683898 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586019 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC8586020 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586021 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)OP(=O…`
ZINC8586022 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC11422512 ZINC	0.800	402.2 Da LogP -1.28 TPSA 197.6	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](OP(=O)(O)O)[C@@H](COP(=O)(O)…`
ZINC95581564 ZINC	0.792	345.4 Da LogP 1.67 TPSA 63.6	✓ Ro5	✓ Clean	`COC(=O)c1cn(C2CC2)c2cc(N3CCNCC3)c(F)cc2c1=O`
ZINC77293473 ZINC	0.780	329.4 Da LogP 1.15 TPSA 94.8	✓ Ro5	✓ Clean	`O=C(O)c1cn(C2CC2)c2cc(N3CCNCC3)c(O)cc2c1=O`
ZINC12503902 ZINC	0.776	326.2 Da LogP -1.57 TPSA 151.1	✓ Ro5	✓ Clean	`O=c1[nH]c(=O)n([C@@H]2C[C@@H](O)[C@@H](COP(=O)(…`
ZINC1529898 ZINC	0.776	326.2 Da LogP -1.57 TPSA 151.1	✓ Ro5	✓ Clean	`O=c1[nH]c(=O)n([C@@H]2C[C@@H](O)[C@H](COP(=O)(O…`
ZINC3871118 ZINC	0.776	326.2 Da LogP -1.57 TPSA 151.1	✓ Ro5	✓ Clean	`O=c1[nH]c(=O)n([C@@H]2C[C@H](O)[C@H](COP(=O)(O)…`
ZINC3875881 ZINC	0.776	326.2 Da LogP -1.57 TPSA 151.1	✓ Ro5	✓ Clean	`O=c1[nH]c(=O)n([C@H]2C[C@H](O)[C@@H](COP(=O)(O)…`
ZINC6090961 ZINC	0.776	387.1 Da LogP -0.94 TPSA 151.1	✓ Ro5	✓ Clean	`O=c1[nH]c(=O)n([C@H]2C[C@H](O)[C@@H](COP(=O)(O)…`
ZINC6524115 ZINC	0.776	326.2 Da LogP -1.57 TPSA 151.1	✓ Ro5	✓ Clean	`O=c1[nH]c(=O)n([C@@H]2C[C@H](O)[C@@H](COP(=O)(O…`
ZINC3789759 ZINC	0.774	345.4 Da LogP 1.97 TPSA 74.6	✓ Ro5	✓ Clean	`C[C@H]1CN(c2cc3c(cc2F)c(=O)c(C(=O)O)cn3C2CC2)CC…`
ZINC5141600 ZINC	0.774	345.4 Da LogP 1.97 TPSA 74.6	✓ Ro5	✓ Clean	`C[C@@H]1CN(c2cc3c(cc2F)c(=O)c(C(=O)O)cn3C2CC2)C…`
ZINC6667024 ZINC	0.766	256.3 Da LogP -0.86 TPSA 93.5	✓ Ro5	✓ Clean	`COC[C@H]1O[C@@H](n2cc(C)c(=O)[nH]c2=O)C[C@@H]1O`
ZINC366933 ZINC	0.765	332.3 Da LogP 2.01 TPSA 71.8	✓ Ro5	✓ Clean	`O=C(O)c1cn(C2CC2)c2cc(N3CCOCC3)c(F)cc2c1=O`
ZINC5850961 ZINC	0.765	345.4 Da LogP 1.93 TPSA 65.8	✓ Ro5	✓ Clean	`CN1CCN(c2cc3c(cc2F)c(=O)c(C(=O)O)cn3C2CC2)CC1`
ZINC169471483 ZINC	0.750	360.3 Da LogP 1.98 TPSA 95.2	✓ Ro5	✓ Clean	`O=NN1CCN(c2cc3c(cc2F)c(=O)c(C(=O)O)cn3C2CC2)CC1`
ZINC3886912 ZINC	0.750	373.4 Da LogP 1.84 TPSA 82.8	✓ Ro5	✓ Clean	`CC(=O)N1CCN(c2cc3c(cc2F)c(=O)c(C(=O)O)cn3C2CC2)…`
ZINC45289474 ZINC	0.750	359.4 Da LogP 2.06 TPSA 63.6	✓ Ro5	✓ Clean	`CCOC(=O)c1cn(C2CC2)c2cc(N3CCNCC3)c(F)cc2c1=O`
ZINC3869839 ZINC	0.745	267.2 Da LogP -1.66 TPSA 139.3	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@@H]2C[C@H](O)[C@H](CO)O2)c(=O)[n…`
ZINC404255 ZINC	0.745	267.2 Da LogP -1.66 TPSA 139.3	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@H]2C[C@@H](O)[C@H](CO)O2)c(=O)[n…`

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 A0A0H3H0Y6

Chemistry

ChEMBL CHEMBL2424893 ChEMBL CHEMBL2165064 ChEMBL CHEMBL2424894 ChEMBL CHEMBL1276635 ChEMBL CHEMBL3702487 ChEMBL CHEMBL430 ChEMBL CHEMBL4530328 ChEMBL CHEMBL202864 ChEMBL CHEMBL203557 ChEMBL CHEMBL4531900 ChEMBL CHEMBL4567626 ChEMBL CHEMBL4438807 ChEMBL CHEMBL4445613 ChEMBL CHEMBL4537564 ChEMBL CHEMBL4570423 ChEMBL CPF