Protein target profile

KP13_01110

Cell division protease ftsH

Genome: KpKP13 Gene: AHE42496.1 ftsH 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GTR0

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Length 644

Pocket druggability 0.765

Direct ligand evidence 0 52 total records

Functional annotation 1 EC 9 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

Independent pocket support: FPocket + P2Rank Both predictors report a high-scoring binding site (FPocket 0.77, P2Rank 0.84). Use the 3D pocket comparison to verify whether they identify the same site. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Strong predicted binding pocket FPocket selected-pocket score 0.77. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.84. 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: Hit
Human identity (%): 58.824 Lower values reduce human off-target concern.
Human E-value: 6.65e-46
Gut microbiome similarity: 59.5% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 97.981 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Localization

Localization: CytoplasmicMembrane

Structure confidence

ColabFold pLDDT: 83.05 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 0.765

Structure A0A0H3GTR0

Pocket Pocket 22

P2Rank 0.839

Structure A0A0H3GTR0

Pocket Pocket 1

ColabFold model

FPocket 0.652 · Pocket 12

P2Rank 0.895 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 2825 / 4744 genomes with a hit

Prevalence 59.5%

Cross-references

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

Sequence

UniProt A0A0H3GTR0

Sequence

Primary amino-acid sequence viewer.

MAKNLILWLVIAVVLMSVFQSFGPSESNGRKVDYSTFLQEVNQDQVREARINGREINVTKKDSNRYTTYIPVNDPKLLDNLLTKNVKVVGEPPEEPSLLASIFISWFPMLLLIGVWIFFMRQMQGGGGKGAMSFGKSKARMLTEDQIKTTFADVAGCDEAKEEVGELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERRSMVMTEAQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLESQISTLYGGRLAEEIIYGPEHVSTGASNDIKVATNLARNMVTQWGFSDKLGPLLYAEEEGEVFLGRSVAKAKHMSDETARIIDQEVKSLIERNYGRARQLLNDNMDILHAMKDALMKYETIDAPQIDDLMARREVRPPAGWEEPGSSNNSDNNGTPRAPRPVDEPRTPNPGNTMSEQLGDK

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Enzyme Commission (EC)

3.4.24.-

Gene Ontology (GO)

GO:0016887 Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
GO:0008270 Binding to a zinc ion (Zn).
GO:0004176 Catalysis of the hydrolysis of peptide bonds, driven by ATP hydrolysis.
GO:0004222 Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.
GO:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
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:0030163 The chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

43 records

Show feature table

Start	End	DB	Term	Name
5	16	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
322	396	FunFam	G3DSA:1.10.8.60:FF:000001	ATP-dependent zinc metalloprotease FtsH
396	599	Gene3D	G3DSA:1.20.58.760	Peptidase M41
396	599	InterPro	IPR037219	Peptidase M41-like
149	319	CDD	cd19501	RecA-like_FtsH
184	323	SMART	SM00382	AAA_5
184	323	InterPro	IPR003593	AAA+ ATPase domain
343	387	Pfam	PF17862	AAA+ lid domain
343	387	InterPro	IPR041569	AAA ATPase, AAA+ lid domain
3	616	Hamap	MF_01458	ATP-dependent zinc metalloprotease FtsH [ftsH].
3	616	InterPro	IPR005936	ATP-dependent zinc metalloprotease, FtsH
322	395	Gene3D	G3DSA:1.10.8.60	-
5	93	Pfam	PF06480	FtsH Extracellular
5	93	InterPro	IPR011546	Peptidase M41, FtsH extracellular
22	97	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
401	591	Pfam	PF01434	Peptidase family M41
401	591	InterPro	IPR000642	Peptidase M41
1	21	SignalP_EUK	SignalP-noTM	SignalP-noTM
141	391	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
141	391	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
138	320	FunFam	G3DSA:3.40.50.300:FF:000001	ATP-dependent zinc metalloprotease FtsH
24	98	Gene3D	G3DSA:3.30.720.210	-
5	24	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
97	119	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
39	595	PANTHER	PTHR23076	METALLOPROTEASE M41 FTSH
17	21	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
9	589	NCBIfam	TIGR01241	ATP-dependent zinc metalloprotease FtsH
9	589	InterPro	IPR005936	ATP-dependent zinc metalloprotease, FtsH
291	309	ProSitePatterns	PS00674	AAA-protein family signature.
291	309	InterPro	IPR003960	ATPase, AAA-type, conserved site
98	119	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
141	320	Gene3D	G3DSA:3.40.50.300	-
141	320	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
120	644	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
397	598	FunFam	G3DSA:1.20.58.760:FF:000001	ATP-dependent zinc metalloprotease FtsH
1	21	Phobius	SIGNAL_PEPTIDE	Signal peptide region
402	602	SUPERFAMILY	SSF140990	FtsH protease domain-like
402	602	InterPro	IPR037219	Peptidase M41-like
24	98	FunFam	G3DSA:3.30.720.210:FF:000001	ATP-dependent zinc metalloprotease FtsH
592	644	MobiDBLite	mobidb-lite	consensus disorder prediction
188	320	Pfam	PF00004	ATPase family associated with various cellular activities (AAA)
188	320	InterPro	IPR003959	ATPase, AAA-type, core
1	4	Phobius	SIGNAL_PEPTIDE_N_REGION	N-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 · FPocket

Druggability: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Site 1 FPocket #22

0.765

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Surrounding area

Site 2 FPocket #24

0.707

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Surrounding area

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.839

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Surrounding area

Site 2 P2Rank #2

0.604

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Surrounding area

Site 3 P2Rank #3

0.057

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Surrounding area

Site 4 P2Rank #4

0.022

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Surrounding area

Residue sets

UniProt: Active site:415-415

UniProt: Binding site:192-199

UniProt: Binding site:414-414

UniProt: Binding site:418-418

UniProt: Binding site:492-492

Binding pockets · FPocket

Druggability: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Site 1 FPocket #12

0.652

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Surrounding area

Site 2 FPocket #39

0.399

Likely same site as P2Rank 3 2.0 Å 14 shared residues 100% of smaller site

Unusual size

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Surrounding area

Site 3 FPocket #38

0.362

Likely same site as P2Rank 5 4.9 Å 9 shared residues 100% of smaller site

Unusual size

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Surrounding area

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.895

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Surrounding area

Site 2 P2Rank #2

0.593

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Surrounding area

Site 3 P2Rank #3

0.111

Likely same site as FPocket 39 2.0 Å 14 shared residues 100% of smaller site

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Surrounding area

Site 4 P2Rank #4

0.092

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Surrounding area

Site 5 P2Rank #5

0.016

Likely same site as FPocket 38 4.9 Å 9 shared residues 100% of smaller site

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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_A0A0H3GTR0	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_01110	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.

52 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 2 records from similar proteins

Structural ligands 2 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

ANP PDB via homolog 506.2 Da · LogP -2.06 · TPSA 281.9 Open detail RCSB PDB

NHX PDB via homolog Detail RCSB PDB

ZINC11688557 ZINC proposed compound · Tanimoto 1.000 Detail ZINC

ZINC3786507 ZINC proposed compound · Tanimoto 1.000 Detail ZINC

ZINC13907320 ZINC proposed compound · Tanimoto 0.828 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
ANP RCSB PDB	5MPB	P33299	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)…`
NHX RCSB PDB	3KDS	Q9WZ49	456.5 Da LogP 1.41 TPSA 150.6	✓ Ro5	✓ Clean	`C[C@@H](C(=O)N)NC(=O)[C@H](Cc1ccc2ccccc2c1)NC(=…`

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
ZINC11688557 ZINC	1.000	456.5 Da LogP 1.41 TPSA 150.6	✓ Ro5	✓ Clean	`CC(C)C[C@@H](CC(=O)NO)C(=O)N[C@@H](Cc1ccc2ccccc…`
ZINC3786507 ZINC	1.000	456.5 Da LogP 1.41 TPSA 150.6	✓ Ro5	✓ Clean	`CC(C)C[C@H](CC(=O)NO)C(=O)N[C@@H](Cc1ccc2ccccc2…`
ZINC13907320 ZINC	0.828	499.6 Da LogP 1.00 TPSA 162.7	1 viol.	✓ Clean	`CC(C)C[C@@H](CC(=O)NO)C(=O)N[C@@H](Cc1ccc2ccccc…`
ZINC3813502 ZINC	0.828	499.6 Da LogP 1.00 TPSA 162.7	1 viol.	✓ Clean	`CC(C)C[C@H](CC(=O)NO)C(=O)N[C@@H](Cc1ccc2ccccc2…`
ZINC44681840 ZINC	0.828	499.6 Da LogP 1.00 TPSA 162.7	1 viol.	✓ Clean	`CC(C)C[C@@H](CC(=O)NO)C(=O)N[C@H](Cc1ccc2ccccc2…`
ZINC44681843 ZINC	0.828	499.6 Da LogP 1.00 TPSA 162.7	1 viol.	✓ Clean	`CC(C)C[C@H](CC(=O)NO)C(=O)N[C@H](Cc1ccc2ccccc2c…`
ZINC95911029 ZINC	0.828	499.6 Da LogP 1.00 TPSA 162.7	1 viol.	✓ Clean	`CC(C)C[C@H](CC(=O)NO)C(=O)N[C@H](Cc1ccc2ccccc2c…`
ZINC98183634 ZINC	0.828	499.6 Da LogP 1.00 TPSA 162.7	1 viol.	✓ Clean	`CC(C)C[C@H](CC(=O)NO)C(=O)N[C@@H](Cc1ccc2ccccc2…`
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(=…`
ZINC13518964 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC1532515 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@H](O…`
ZINC1571045 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC1842158 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@H](O…`
ZINC2046931 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC2126310 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3201891 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC3201893 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3830180 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3860156 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3977897 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](COP(=O)(O)O)[C@@H](O…`
ZINC4806442 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC8613167 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC35850116 ZINC	0.729	456.5 Da LogP 1.41 TPSA 150.6	✓ Ro5	✓ Clean	`CC(C)C[C@H](CC(=O)NO)C(=O)N[C@@H](Cc1cccc2ccccc…`
ZINC4096224 ZINC	0.729	346.2 Da LogP -1.90 TPSA 191.9	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](N)(=O)O)[C@@…`
ZINC12503850 ZINC	0.726	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC141161066 ZINC	0.726	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC141163786 ZINC	0.726	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC4228246 ZINC	0.726	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OS(=O…`
ZINC105372833 ZINC	0.712	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@H](O…`
ZINC105372837 ZINC	0.712	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@H](O…`
ZINC17107643 ZINC	0.712	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC204538551 ZINC	0.712	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC1560408734 ZINC	0.708	498.6 Da LogP 1.17 TPSA 162.7	1 viol.	✓ Clean	`C[C](NC(=O)[C@@H](Cc1ccc2ccccc2c1)NC(=O)[C@H](C…`
ZINC1560408735 ZINC	0.708	498.6 Da LogP 1.17 TPSA 162.7	1 viol.	✓ Clean	`C[C](NC(=O)[C@@H](Cc1ccc2ccccc2c1)NC(=O)[C@@H](…`
ZINC31475423 ZINC	0.703	434.3 Da LogP -2.99 TPSA 238.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@@](=O)(O)OC(=O)…`
ZINC1532902 ZINC	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@@](O)(CC(=O)O)C(=O)O`
ZINC2018106 ZINC	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@](O)(CC(=O)O)C(=O)O`
ZINC117292468 ZINC	0.697	499.6 Da LogP 1.09 TPSA 167.8	✓ Ro5	✓ Clean	`CC(C)C[C@H](CC(=O)NO)C(=O)N[C@@H](Cc1ccc2ccccc2…`
ZINC642881691 ZINC	0.697	499.6 Da LogP 1.09 TPSA 167.8	✓ Ro5	✓ Clean	`CC(C)C[C@@H](CC(=O)NO)C(=O)N[C@@H](Cc1ccc2ccccc…`
ZINC13527614 ZINC	0.694	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)CP(=O)…`

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.