KpATCC43816 Protein target profile

transcription-repair coupling factor

Accession: VK055_1352

Gene: mfd AIK79975.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A0H3GMV4

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Length 1148

Pocket druggability (P2Rank · AlphaFold DB model) 0.901

Direct ligand evidence 0 51 total records

Functional annotation 1 EC 9 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: P2Rank + FPocket Both predictors report a high-scoring binding site (P2Rank 0.90, FPocket 0.89). Use the 3D pocket comparison to verify whether they identify the same site. No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Strong predicted binding pocket FPocket selected-pocket score 0.89. This is a computational pocket signal, not binding validation. 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: No hit
Gut microbiome similarity: 3.5% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 63.772 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 83.33 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) 0.901

Structure A0A0H3GMV4

Pocket Pocket 1

Druggability (FPocket) 0.894

Structure A0A0H3GMV4

Pocket Pocket 95

ColabFold model

P2Rank 0.975 · Pocket 1

FPocket 0.39 · Pocket 22

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 166 / 4744 genomes with a hit

Prevalence 3.5%

Metabolic context

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

This protein is not associated with the imported metabolic network for this genome.

Browse the genome's metabolic network

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MPEQYRYSLPVKAGDQRQLGELTGAACATLVAEMAERHKGPVVLVAPDMQNALRLNDEIRQFTDSMVMGLADWETLPYDSFSPHQDIISSRLATLYQLPTMQRGVLIVPVSTLMQRVCPHSFLHGHALVMKKGQRLSRDALRDQLEGAGYRHVDQVMEHGEYATRGALLDLFPMGSDQPYRLDFFDDEIDSLRLFDVDSQRTLEEVAAINLLPAHEFPTDQTAIELFRSQWRDRFEVKRDAEHIYQQVSKGTLPAGIEYWQPLFFSEPLPPLFSYFPASTLIVNTGDLEASAERFQNEARARFENRGVDPMRPLLPPELLWLRSDELFSELKKWPRVQLKTERLADKAANTNLGYQTLPDLAVQAQNKAPLDNLRRFLESFTGPVIFSVESEGRREALSEMLARIKVAPKHVLRLEEATGNGRYLMIGAAEHGFIDSQRGLALICESDLLGERVARRRQDSRRTINPDTLIRNLAELHIGQPVVHLEHGVGRYAGMTTLEAGGITGEYLMLTYANDAKLYVPVSSLHLISRYAGGAEENAPLHKLGGDAWTRARQKAAEKVRDVAAELLDIYAQRAAKAGFAFKHDREQYQLFCDGFPFETTPDQAQAINAVLSDMCQPLAMDRLVCGDVGFGKTEVAMRAAFLAVENHKQVAVLVPTTLLAQQHYDNFRDRFANWPVRIEMLSRFRSAKEQAQILEQAAEGKIDILIGTHKLLQSEVKLRDLGLLIVDEEHRFGVRHKERIKAMRADVDILTLTATPIPRTLNMAMSGMRDLSIIATPPARRLAVKTFVREYDALVVREAILRETLRGGQVYYLFNDVENIQKAADKLAELVPEARIAIGHGQMRERELERVMNDFHHQRFNVLVCTTIIETGIDIPTANTIIIERADHFGLAQLHQLRGRVGRSHHQAYAWLLTPHPKAMTTDAQKRLEAIASLEDLGAGFALATHDLEIRGAGELLGEDQSGQMETIGFSLYMELLENAVDALKAGREPSLEDLTSQQTEVELRMPSLLPDDFIPDVNTRLSFYKRIASAKNEQDLEEIKVELIDRFGRLPDAARNLLDIARLRQQAQKLGIRKLESNEKGGVIEFNEKNNVNPVWLIGLLQKQPQHFRLDGPTRLKFMQDLEERKTRMDWVRQFMRQLEENAVA

MPEQYRYSLPVKAGDQRQLGELTGAACATLVAEMAERHKGPVVLVAPDMQNALRLNDEIRQFTDSMVMGLADWETLPYDSFSPHQDIISSRLATLYQLPTMQRGVLIVPVSTLMQRVCPHSFLHGHALVMKKGQRLSRDALRDQLEGAGYRHVDQVMEHGEYATRGALLDLFPMGSDQPYRLDFFDDEIDSLRLFDVDSQRTLEEVAAINLLPAHEFPTDQTAIELFRSQWRDRFEVKRDAEHIYQQVSKGTLPAGIEYWQPLFFSEPLPPLFSYFPASTLIVNTGDLEASAERFQNEARARFENRGVDPMRPLLPPELLWLRSDELFSELKKWPRVQLKTERLADKAANTNLGYQTLPDLAVQAQNKAPLDNLRRFLESFTGPVIFSVESEGRREALSEMLARIKVAPKHVLRLEEATGNGRYLMIGAAEHGFIDSQRGLALICESDLLGERVARRRQDSRRTINPDTLIRNLAELHIGQPVVHLEHGVGRYAGMTTLEAGGITGEYLMLTYANDAKLYVPVSSLHLISRYAGGAEENAPLHKLGGDAWTRARQKAAEKVRDVAAELLDIYAQRAAKAGFAFKHDREQYQLFCDGFPFETTPDQAQAINAVLSDMCQPLAMDRLVCGDVGFGKTEVAMRAAFLAVENHKQVAVLVPTTLLAQQHYDNFRDRFANWPVRIEMLSRFRSAKEQAQILEQAAEGKIDILIGTHKLLQSEVKLRDLGLLIVDEEHRFGVRHKERIKAMRADVDILTLTATPIPRTLNMAMSGMRDLSIIATPPARRLAVKTFVREYDALVVREAILRETLRGGQVYYLFNDVENIQKAADKLAELVPEARIAIGHGQMRERELERVMNDFHHQRFNVLVCTTIIETGIDIPTANTIIIERADHFGLAQLHQLRGRVGRSHHQAYAWLLTPHPKAMTTDAQKRLEAIASLEDLGAGFALATHDLEIRGAGELLGEDQSGQMETIGFSLYMELLENAVDALKAGREPSLEDLTSQQTEVELRMPSLLPDDFIPDVNTRLSFYKRIASAKNEQDLEEIKVELIDRFGRLPDAARNLLDIARLRQQAQKLGIRKLESNEKGGVIEFNEKNNVNPVWLIGLLQKQPQHFRLDGPTRLKFMQDLEERKTRMDWVRQFMRQLEENAVA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

3.6.4.-

Gene Ontology (GO)

GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0006281 The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.
GO:0003676 Binding to a nucleic acid.
GO:0003684 Binding to damaged DNA.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0003678 Unwinding of a DNA helix, driven by ATP hydrolysis.
GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.
GO:0006355 Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription.
GO:0000716 The identification of lesions on the actively transcribed strand of the DNA duplex as well as a small subset of lesions not recognized by the general nucleotide-excision repair pathway.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

57 records

Show feature table

Start	End	DB	Term	Name
1006	1097	Pfam	PF03461	TRCF domain
1006	1097	InterPro	IPR005118	Transcription-repair-coupling factor, C-terminal domain
475	987	Gene3D	G3DSA:3.40.50.300	-
475	987	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
9	340	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
9	340	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
577	984	PANTHER	PTHR47964	ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC
577	984	InterPro	IPR047112	ATP-dependent DNA helicase RecG/Transcription-repair-coupling factor
148	1079	NCBIfam	TIGR00580	transcription-repair coupling factor
148	1079	InterPro	IPR004576	Transcription-repair coupling factor
128	213	FunFam	G3DSA:3.30.2060.10:FF:000002	Transcription-repair-coupling factor
520	780	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
520	780	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
24	335	Gene3D	G3DSA:3.40.50.11180	-
480	538	Gene3D	G3DSA:2.40.10.170	-
1005	1105	SMART	SM00982	TRCF_a_2_a
1005	1105	InterPro	IPR005118	Transcription-repair-coupling factor, C-terminal domain
797	951	ProSiteProfiles	PS51194	Superfamilies 1 and 2 helicase C-terminal domain profile.
797	951	InterPro	IPR001650	Helicase, C-terminal
477	572	Pfam	PF02559	CarD-like/TRCF domain
477	572	InterPro	IPR003711	CarD-like/TRCF, RNAP-interacting domain
129	217	Pfam	PF17757	UvrB interaction domain
129	217	InterPro	IPR041471	UvrB, interaction domain
467	545	SUPERFAMILY	SSF141259	CarD-like
467	545	InterPro	IPR036101	CarD-like/TRCF, RNAP-interacting domain superfamily
476	573	SMART	SM01058	CarD_TRCF_2
476	573	InterPro	IPR003711	CarD-like/TRCF, RNAP-interacting domain
615	776	ProSiteProfiles	PS51192	Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile.
615	776	InterPro	IPR014001	Helicase superfamily 1/2, ATP-binding domain
354	450	Gene3D	G3DSA:3.40.50.11140	-
777	987	FunFam	G3DSA:3.40.50.300:FF:000300	Transcription-repair-coupling factor
1001	1148	FunFam	G3DSA:3.90.1150.50:FF:000001	Transcription-repair-coupling factor
992	1144	SUPERFAMILY	SSF143517	TRCF domain-like
992	1144	InterPro	IPR037235	TRCF-like, C-terminal D7 domain
597	787	SMART	SM00487	ultradead3
597	787	InterPro	IPR014001	Helicase superfamily 1/2, ATP-binding domain
539	776	FunFam	G3DSA:3.40.50.300:FF:000546	Transcription-repair-coupling factor
586	778	CDD	cd17991	DEXHc_TRCF
802	906	Pfam	PF00271	Helicase conserved C-terminal domain
802	906	InterPro	IPR001650	Helicase, C-terminal
779	987	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
779	987	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
602	762	Pfam	PF00270	DEAD/DEAH box helicase
602	762	InterPro	IPR011545	DEAD/DEAH box helicase domain
28	1127	Hamap	MF_00969	Transcription-repair-coupling factor [mfd].
28	1127	InterPro	IPR004576	Transcription-repair coupling factor
539	778	Gene3D	G3DSA:3.40.50.300	-
539	778	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
785	935	CDD	cd18810	SF2_C_TRCF
1001	1148	Gene3D	G3DSA:3.90.1150.50	-
1001	1148	InterPro	IPR037235	TRCF-like, C-terminal D7 domain
823	907	SMART	SM00490	helicmild6
823	907	InterPro	IPR001650	Helicase, C-terminal
351	463	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
351	463	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
128	213	Gene3D	G3DSA:3.30.2060.10	-
480	538	FunFam	G3DSA:2.40.10.170:FF:000007	Transcription-repair-coupling factor

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

0.901

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Surrounding area

Pocket 2 P2Rank #2

0.561

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Surrounding area

Pocket 3 P2Rank #3

0.55

Likely same site as FPocket 95 3.9 Å 12 shared residues 86% of smaller site

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Surrounding area

Pocket 4 P2Rank #4

0.418

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Surrounding area

Pocket 5 P2Rank #5

0.342

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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 #95

0.894

Likely same site as P2Rank 3 3.9 Å 12 shared residues 86% of smaller site

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Surrounding area

Pocket 2 FPocket #104

0.469 Unusual size

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Surrounding area

Pocket 3 FPocket #59

0.257

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Surrounding area

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.975

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Surrounding area

Pocket 2 P2Rank #2

0.898

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Surrounding area

Pocket 3 P2Rank #3

0.496

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Surrounding area

Pocket 4 P2Rank #4

0.418

Likely same site as FPocket 22 0.6 Å 17 shared residues 100% of smaller site

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Surrounding area

Pocket 5 P2Rank #5

0.342

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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_A0A0H3GMV4	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_1352	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.

51 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 1 records from similar proteins

Structural ligands 1 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

AGS PDB via homolog 523.2 Da · LogP -1.51 · TPSA 262.1 Open detail RCSB PDB

ZINC12360002 ZINC proposed compound · Tanimoto 0.855 Detail ZINC

ZINC12360703 ZINC proposed compound · Tanimoto 0.855 Detail ZINC

ZINC12503599 ZINC proposed compound · Tanimoto 0.855 Detail ZINC

ZINC16546165 ZINC proposed compound · Tanimoto 0.855 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
AGS RCSB PDB	6M6B	Q72KB4	523.2 Da LogP -1.51 TPSA 262.1	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`

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
ZINC12360002 ZINC	0.855	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	0.855	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	0.855	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	0.855	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	0.855	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	0.855	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	0.855	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	0.855	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	0.855	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	0.855	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	0.855	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	0.782	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	0.782	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	0.782	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	0.782	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	0.782	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	0.782	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	0.782	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	0.782	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	0.782	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	0.782	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	0.782	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	0.782	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	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC4096224 ZINC	0.768	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	0.763	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	0.763	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	0.763	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	0.763	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	0.750	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	0.750	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	0.750	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	0.750	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC31475423 ZINC	0.738	434.3 Da LogP -2.99 TPSA 238.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@@](=O)(O)OC(=O)…`
ZINC31516918 ZINC	0.730	446.4 Da LogP -1.33 TPSA 218.2	1 viol.	✓ Clean	`CC(C)[C@H](N)C(=O)O[P@](=O)(O)OC[C@H]1O[C@@H](n…`
ZINC105469665 ZINC	0.729	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)CP(=O…`
ZINC13527614 ZINC	0.729	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)CP(=O)…`
ZINC219330894 ZINC	0.729	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873852 ZINC	0.729	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873853 ZINC	0.729	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@](=O)(O)CP(=O…`
ZINC3873854 ZINC	0.729	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873855 ZINC	0.729	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@](=O)(O)CP(=O…`
ZINC5615251 ZINC	0.712	375.3 Da LogP -0.55 TPSA 164.1	1 viol.	✓ Clean	`COP(=O)(OC)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@…`
ZINC5615253 ZINC	0.712	375.3 Da LogP -0.55 TPSA 164.1	1 viol.	✓ Clean	`COP(=O)(OC)OC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)[C…`
ZINC5615258 ZINC	0.712	375.3 Da LogP -0.55 TPSA 164.1	1 viol.	✓ Clean	`COP(=O)(OC)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@…`
ZINC5615263 ZINC	0.712	375.3 Da LogP -0.55 TPSA 164.1	1 viol.	✓ Clean	`COP(=O)(OC)OC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)[C…`
ZINC1582675 ZINC	0.700	403.3 Da LogP 0.23 TPSA 164.1	1 viol.	✓ Clean	`CCOP(=O)(OCC)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[…`
ZINC5486730 ZINC	0.700	403.3 Da LogP 0.23 TPSA 164.1	1 viol.	✓ Clean	`CCOP(=O)(OCC)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[…`
ZINC5486734 ZINC	0.700	403.3 Da LogP 0.23 TPSA 164.1	1 viol.	✓ Clean	`CCOP(=O)(OCC)OC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)…`
ZINC5486740 ZINC	0.700	403.3 Da LogP 0.23 TPSA 164.1	1 viol.	✓ Clean	`CCOP(=O)(OCC)OC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)…`

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 A0A0H3GMV4