Protein target profile

KP13_00684

Ferrous iron transport protein B

Genome: KpKP13 Gene: AHE42304.1 feoB 3D evidence: Experimental + AlphaFold DB model + ColabFold model UniProt A6TF32

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Length 772

Pocket druggability 0.993

Direct ligand evidence 1 58 total records

Functional annotation 0 EC 4 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

Independent pocket support: FPocket + P2Rank Both predictors report a high-scoring binding site (FPocket 0.99, P2Rank 0.95). Use the 3D pocket comparison to verify whether they identify the same site. Experimental structure available At least one PDB experimental structure is loaded, not just a predicted model - stronger structural coverage than AlphaFold/ColabFold alone. Direct ligand evidence 1 direct ligand records. Strong known ligand: co-crystal structure 1 PDB record(s) show a ligand actually co-crystallized with this exact protein - real experimental evidence, not a computational prediction. 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: 2.4% 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: CytoplasmicMembrane

Structure confidence

ColabFold pLDDT: 82.6 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 0.993

Structure A6TF32

Pocket Pocket 16

P2Rank 0.952

Structure A6TF32

Pocket Pocket 1

ColabFold model

FPocket 0.971 · Pocket 63

P2Rank 0.863 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 112 / 4744 genomes with a hit

Prevalence 2.4%

Cross-references

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

Sequence

UniProt A6TF32

Structure

PDB 2WIA PDB 2WIB PDB 2WIC

Sequence

Primary amino-acid sequence viewer.

MQKLTVGLIGNPNSGKTTLFNQLTGARQRVGNWAGVTVERKEGIFATTDHQVTLVDLPGTYSLTTISSQTSLDEQIACHYILSGDADMLINVVDASNLERNLYLTLQLLELGIPCVVALNMLDIAEKQQVRIDIDALAARLGCPVIPLVSTRGRGIEALKIALDRHQANSDLELVHYPQPLLREADLLAQQMSAQIPTRQRRWLGLQMLEGDIYSRAYAGDAADKLDIALANLSDEIDDPALHIADARYQTIAAICDAVSNTLTAEPSRFTAAMDKVILNRFLGLPIFLFVMYLMFLLAINIGGALQPIFDAGSVAIFVHGIQWLGYALHFPDWLTVFLAQGIGGGINTVLPLVPQIGMMYLFLSFLEDSGYMARAAFVMDRLMQALGLPGKSFVPLIVGFGCNVPSVMGARTLDAPRERLMTIMMAPFMSCGARLAIFAVFAAAFFGQNGALAVFSLYVLGIVMAILTGLMLKHTIMRGEASPFVMELPVYHVPHIKSLIIQTWQRLKGFVLRAGKVIVIVSIFLSALNSFSLSGKVVDNINDSALASVSRVITPVFKPIGVHEDNWQATVGLFTGAMAKEVVVGTLNTLYTAEDIQNEEFNPQTFSLGEELLAAVDETWQGLKDTFSLSVLANPIEASKGDGEMATGAMGVMGSKFGSAAAAYSYLIFVLLYIPCISVMGAIARESSRGWMTFSILWGLNIAYSLSTLYYQTVSFSDHPRYSLVCILAVVLFNVVLFGLLRRARSRVDVSLLATRKTPASCCSSPAGDCH

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

4 GO

Gene Ontology (GO)

GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
GO:0015093 Enables the transfer of ferrous iron (Fe(II) or Fe2+) ions from one side of a membrane to the other.
GO:0006826 The directed movement of iron (Fe) ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
GO:0005525 Binding to GTP, guanosine triphosphate.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

58 records

Show feature table

Start	End	DB	Term	Name
455	507	Pfam	PF07664	Ferrous iron transport protein B C terminus
455	507	InterPro	IPR011640	Ferrous iron transport protein B, C-terminal
743	772	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
511	529	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
27	45	PRINTS	PR00326	GTP1/OBG GTP-binding protein family signature
27	45	InterPro	IPR006073	GTP binding domain
6	26	PRINTS	PR00326	GTP1/OBG GTP-binding protein family signature
6	26	InterPro	IPR006073	GTP binding domain
179	259	Pfam	PF17910	FeoB cytosolic helical domain
179	259	InterPro	IPR041069	FeoB, cytosolic helical domain
723	742	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
415	425	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
277	299	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
686	691	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
309	331	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
530	663	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
691	713	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
282	306	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
448	452	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
365	393	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
386	408	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
175	274	Gene3D	G3DSA:1.10.287.1770	-
429	447	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
312	331	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
1	174	Gene3D	G3DSA:3.40.50.300	-
1	174	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
1	719	PANTHER	PTHR43185	FERROUS IRON TRANSPORT PROTEIN B
474	510	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
451	473	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
712	722	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
344	366	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
5	160	Pfam	PF02421	Ferrous iron transport protein B
5	160	InterPro	IPR030389	FeoB-type guanine nucleotide-binding (G) domain
394	414	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
307	311	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
510	532	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
332	342	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
664	685	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
4	167	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
4	167	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
723	742	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
3	175	FunFam	G3DSA:3.40.50.300:FF:000426	Ferrous iron transport protein B
10	687	NCBIfam	TIGR00437	ferrous iron transport protein B
10	687	InterPro	IPR003373	Ferrous iron transport protein B
3	169	ProSiteProfiles	PS51711	FeoB-type guanine nucleotide-binding (G) domain profile.
3	169	InterPro	IPR030389	FeoB-type guanine nucleotide-binding (G) domain
1	281	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
453	473	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
692	711	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
662	684	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
343	364	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
353	443	Pfam	PF07670	Nucleoside recognition
353	443	InterPro	IPR011642	Nucleoside transporter/FeoB GTPase, Gate domain
512	689	Pfam	PF07670	Nucleoside recognition
512	689	InterPro	IPR011642	Nucleoside transporter/FeoB GTPase, Gate domain
8	165	CDD	cd01879	FeoB
8	165	InterPro	IPR030389	FeoB-type guanine nucleotide-binding (G) domain
426	447	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.

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

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

Site 1 P2Rank #1

0.314

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Surrounding area

Site 2 P2Rank #2

0.177

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Surrounding area

Site 3 P2Rank #3

0.164

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Surrounding area

Site 4 P2Rank #4

0.055

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Surrounding area

Site 5 P2Rank #5

0.016

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Surrounding area

Binding pockets · FPocket

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

Site 1 FPocket #16

0.993

Likely same site as P2Rank 1 4.3 Å 25 shared residues 71% of smaller site

Unusual size

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Surrounding area

Site 2 FPocket #39

0.964

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Surrounding area

Site 3 FPocket #38

0.882

Likely same site as P2Rank 5 2.5 Å 14 shared residues 100% of smaller site

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Surrounding area

Site 4 FPocket #6

0.845

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

0.952

Likely same site as FPocket 16 4.3 Å 25 shared residues 71% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.462

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Surrounding area

Site 3 P2Rank #3

0.371

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Surrounding area

Site 4 P2Rank #4

0.307

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Surrounding area

Site 5 P2Rank #5

0.222

Likely same site as FPocket 38 2.5 Å 14 shared residues 100% of smaller site

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Surrounding area

Residue sets

UniProt: Binding site:10-17

UniProt: Binding site:120-123

UniProt: Binding site:121-121

UniProt: Binding site:123-123

UniProt: Binding site:13-13

UniProt: Binding site:133-133

UniProt: Binding site:14-14

UniProt: Binding site:149-151

UniProt: Binding site:15-15

UniProt: Binding site:150-150

UniProt: Binding site:16-16

UniProt: Binding site:17-17

UniProt: Binding site:18-18

UniProt: Binding site:21-21

UniProt: Binding site:24-24

UniProt: Binding site:25-25

UniProt: Binding site:35-39

UniProt: Binding site:56-59

All structural evidence 3 experimental · 2 predicted

Structural evidence

3 + 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
PDB 2WIA	X-ray	—	A	—	PDBe RCSB PDBj File	Viewing
PDB 2WIB	X-ray	—	A	—	PDBe RCSB PDBj File	Loaded
PDB 2WIC	X-ray	—	A	—	PDBe RCSB PDBj File	Loaded
AlphaFold DB AF_A6TF32	AlphaFold DB	—	—	full sequence	—	Loaded
ColabFold KP13_00684	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.

58 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 1 same-protein records

Transferred evidence 7 records from similar proteins

Structural ligands 8 1 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

GNP PDB co-crystal 522.2 Da · LogP -2.76 · TPSA 301.9 Open detail RCSB PDB

AGO PDB via homolog Detail RCSB PDB

ALF PDB via homolog Detail RCSB PDB

BGO PDB via homolog Detail RCSB PDB

FLC 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.

Ligand	Source crystal	MW · LogP · TPSA	Lipinski	PAINS	SMILES
GNP RCSB PDB	2WIC Open crystal	522.2 Da LogP -2.76 TPSA 301.9	3 viol.	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O…`

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
AGO RCSB PDB	3HYT	P33650	653.3 Da LogP -0.65 TPSA 316.8	3 viol.	✓ Clean	`CNc1ccccc1C(=O)O[C@@H]2[C@H](O[C@H](C2=O)n3cnc4…`
ALF RCSB PDB	3SS8	Q5M586	103.0 Da LogP 1.30 TPSA 0.0	✓ Ro5	✓ Clean	`F[Al-](F)(F)F`
BGO RCSB PDB	3TAH	Q5M586	576.4 Da LogP -0.55 TPSA 270.7	3 viol.	✓ Clean	`CNc1ccccc1C(=O)O[C@@H]2[C@H](O[C@H]([C@@H]2O)n3…`
FLC RCSB PDB	2WJH	Q57986	189.1 Da LogP -5.25 TPSA 140.6	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O`
GCP RCSB PDB	3I92	P33650	521.2 Da LogP -2.22 TPSA 289.9	3 viol.	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O…`
GGM RCSB PDB	3B1V	Q5M586	655.3 Da LogP -0.86 TPSA 320.0	3 viol.	✓ Clean	`CNc1ccccc1C(=O)O[C@@H]2[C@H](O[C@H]([C@@H]2O)n3…`
GNH RCSB PDB	4R98	P33650	442.2 Da LogP -2.49 TPSA 258.4	2 viol.	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=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
ZINC104869865 ZINC	0.836	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O…`
ZINC12504289 ZINC	0.836	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC34541308 ZINC	0.836	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC35000839 ZINC	0.836	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC45284491 ZINC	0.836	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC80639694 ZINC	0.836	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC8215481 ZINC	0.836	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC12501413 ZINC	0.770	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)…`
ZINC12958448 ZINC	0.770	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](COP(=O)(O)O)[C@H](O)[…`
ZINC1532555 ZINC	0.770	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[…`
ZINC16546189 ZINC	0.770	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](COP(=O)(O)O)[C@H](O)[…`
ZINC2159505 ZINC	0.770	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)…`
ZINC3073318 ZINC	0.770	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)…`
ZINC3869963 ZINC	0.770	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)…`
ZINC3869965 ZINC	0.770	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@@H](COP(=O)(O)O)[C@@H](O…`
ZINC9334496 ZINC	0.770	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[…`
ZINC71774763 ZINC	0.671	432.3 Da LogP -2.23 TPSA 198.3	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@](=O)(O)N3CCOCC3…`
ZINC4743771 ZINC	0.652	361.3 Da LogP -2.70 TPSA 182.6	1 viol.	✓ Clean	`CS(=O)(=O)OC[C@H]1O[C@@H](n2cnc3c(=O)[nH]c(N)nc…`
ZINC4743772 ZINC	0.652	361.3 Da LogP -2.70 TPSA 182.6	1 viol.	✓ Clean	`CS(=O)(=O)OC[C@@H]1O[C@@H](n2cnc3c(=O)[nH]c(N)n…`
ZINC4743774 ZINC	0.652	361.3 Da LogP -2.70 TPSA 182.6	1 viol.	✓ Clean	`CS(=O)(=O)OC[C@H]1O[C@@H](n2cnc3c(=O)[nH]c(N)nc…`
ZINC4743775 ZINC	0.652	361.3 Da LogP -2.70 TPSA 182.6	1 viol.	✓ Clean	`CS(=O)(=O)OC[C@@H]1O[C@@H](n2cnc3c(=O)[nH]c(N)n…`
ZINC12503703 ZINC	0.638	427.2 Da LogP -1.42 TPSA 232.3	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2C[C@H](O)[C@@H](CO[P@@](=O)(…`
ZINC8215878 ZINC	0.638	427.2 Da LogP -1.42 TPSA 232.3	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2C[C@H](O)[C@@H](CO[P@@](=O)(O…`
ZINC100058967 ZINC	0.632	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc(=O)c2ncn([C@H]3O[C@H](CO[P@](=O)(O)OP(=O)…`
ZINC12504287 ZINC	0.632	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc(=O)c2ncn([C@@H]3O[C@@H](CO[P@@](=O)(O)OP(…`
ZINC12504288 ZINC	0.632	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc(=O)c2ncn([C@H]3O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC31308647 ZINC	0.632	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc(=O)c2ncn([C@@H]3O[C@@H](CO[P@@](=O)(O)OP(…`
ZINC1532637 ZINC	0.629	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](CO)[C@H](O)[C@@H]2O)c…`
ZINC1550030 ZINC	0.629	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO)[C@@H](O)[C@H]2O)c…`
ZINC1570863 ZINC	0.629	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@H](CO)[C@@H](O)[C@H]2O)c(…`
ZINC1698205 ZINC	0.629	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@H](CO)[C@@H](O)[C@@H]2O)c…`
ZINC2020098 ZINC	0.629	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](CO)[C@H](O)[C@H]2O)c(…`
ZINC38580950 ZINC	0.629	282.3 Da LogP -2.72 TPSA 165.3	✓ Ro5	✓ Clean	`NC[C@H]1O[C@@H](n2cnc3c(=O)[nH]c(N)nc32)[C@H](O…`
ZINC3869967 ZINC	0.629	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](CO)[C@@H](O)[C@H]2O)c…`
ZINC3869968 ZINC	0.629	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@@H](CO)[C@@H](O)[C@H]2O)…`
ZINC3869969 ZINC	0.629	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](CO)[C@@H](O)[C@@H]2O)…`
ZINC3869970 ZINC	0.629	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@@H](CO)[C@@H](O)[C@@H]2O…`
ZINC4990799 ZINC	0.629	282.3 Da LogP -2.72 TPSA 165.3	✓ Ro5	✓ Clean	`NC[C@@H]1O[C@H](n2cnc3c(=O)[nH]c(N)nc32)[C@H](O…`
ZINC4990800 ZINC	0.629	282.3 Da LogP -2.72 TPSA 165.3	✓ Ro5	✓ Clean	`NC[C@@H]1O[C@@H](n2cnc3c(=O)[nH]c(N)nc32)[C@H](…`
ZINC4990801 ZINC	0.629	282.3 Da LogP -2.72 TPSA 165.3	✓ Ro5	✓ Clean	`NC[C@@H]1O[C@H](n2cnc3c(=O)[nH]c(N)nc32)[C@@H](…`
ZINC4990802 ZINC	0.629	282.3 Da LogP -2.72 TPSA 165.3	✓ Ro5	✓ Clean	`NC[C@@H]1O[C@@H](n2cnc3c(=O)[nH]c(N)nc32)[C@@H]…`
ZINC5605239 ZINC	0.629	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@@H](CO)[C@H](O)[C@H]2O)c…`
ZINC6119283 ZINC	0.629	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO)[C@H](O)[C@H]2O)c(…`
ZINC6585367 ZINC	0.629	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO)[C@@H](O)[C@@H]2O)…`
ZINC8613125 ZINC	0.629	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO)[C@H](O)[C@@H]2O)c…`
ZINC97973759 ZINC	0.629	282.3 Da LogP -2.72 TPSA 165.3	✓ Ro5	✓ Clean	`NC[C@H]1O[C@@H](n2cnc3c(=O)[nH]c(N)nc32)[C@H](O…`
ZINC97973760 ZINC	0.629	282.3 Da LogP -2.72 TPSA 165.3	✓ Ro5	✓ Clean	`NC[C@H]1O[C@@H](n2cnc3c(=O)[nH]c(N)nc32)[C@@H](…`
ZINC35024785 ZINC	0.627	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)O…`
ZINC4261903 ZINC	0.627	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)O…`
ZINC95921560 ZINC	0.627	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)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.