KpKP13 Protein target profile

Helicase superfamily protein

Accession: KP13_01338

Gene: AHE46598.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A6A8EMP7

Export view

Length 1180

Pocket druggability (P2Rank · AlphaFold DB model) 0.94

Direct ligand evidence 0 57 total records

Functional annotation 0 EC 4 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: P2Rank + FPocket Both predictors report a high-scoring binding site (P2Rank 0.94, FPocket 0.88). Use the 3D pocket comparison to verify whether they identify the same site. Strong predicted binding pocket FPocket selected-pocket score 0.88. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.94. Structure available AlphaFold DB model + ColabFold model 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 (%): 36.111 Lower values reduce human off-target concern.
Human E-value: 7.57e-08
Gut microbiome similarity: 0.2% 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.

Structure confidence

ColabFold pLDDT: 85.53 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) 0.94

Structure A0A6A8EMP7

Pocket Pocket 1

Druggability (FPocket) 0.883

Structure A0A6A8EMP7

Pocket Pocket 22

ColabFold model

P2Rank 0.986 · Pocket 1

FPocket 0.312 · Pocket 82

Core conservation Accessory gene

Roary accessory

CoreCruncher accessory

Gut microbiome 11 / 4744 genomes with a hit

Prevalence 0.2%

Sequence

Primary amino-acid sequence viewer.

MLKLEEIKKDAQVRGIVEGQVVRVVTVEQIGEHALTVYYKDSKGVLAERMLFRSDEMALELATVGRAWAFDADGGDFKLGLEAYRISQAALFDPMMAVNMANVDPLPHQISAVYEYMLPKQPLRYVLADDPGAGKTIMAGLFISELLLRADARRIMVVSPGSLTEQWQDELFEKFGLQFEIFSKEKQEQCATGNFFTETDRLICRLDQLSRSEELQEKLRNTDWDLIIVDEAHKLSANYFGNKINKTKRFALGELLGSICRHFLLMTATPHNGKEEDFQVWMSLLDSDRFYGKFREGAHKVDITDMMRRMVKEELLTFDGTPLFPERRAYTANYDLSSLEASLYEQVTTYVREEMNRADKLDNKKKNTVGFALTQLQRRLASSPEAIYQSLKRRRNRLKDKLAEMKLLARGQKAKLTGVAETLGSYTVTKQLDLPDNWDELDEDLSAEEYELYAEQVADQATAAETILELDAEILSLKDLEQQALLLVQSGNDKKWEQLSALLQDSPEMKNRDGSRRKLIIFTEHKDTLNYLRQRVGDLLGQSNAVRVIYGGTNRDERRKIQSEFRSDPTVLVLIATDAAGEGVNLQNANLMVNYDLPWNPNRLEQRFGRIHRIGQKEVCHLWNIVANETREGEVFQKLFAKLEIEKQALGGKVFDILGEAFDNVSLKQLLMDAIRYGEDPAVRARMDQAIEGALDSDHLKEIMRRNALVESHMGMEGLYAIKEQMEKAEARRLQPFFIRAFFQEAFQMLGGDLREREQGRYEIRHVPAVIRERDRTIGESRTPVLPRYERVCFEKQLTRPTGKVLAELLHPVHPLMHSVLDLTLQAHRGKLKQGAVLVDPADDCDEPRLIIMLEHSVRETAEQAKSIASRRLQFVAIDKACQASYAGWAPHLDLVPISEGDLTLVQDILCSPWLSQPLEPLALQLASEKLVPEHFAEVKTRRELQADKTLAAVHERLIKEINYWQDRYLKLSDDVKSGKQPRMQPENARRRVDELTARLQQRTTELTALKQVVSSTPVVIGSALVIPQGLLAKRKGEVMFSPDAASRAHIERVAMQAVTDAEQALGHMVIDVAADKCGWDITARPPLKSDGSLPQDRHIEVKGRSKGQITITVSRNEILYALNQADKFLLAIVLVEGDKAEGPYYIRQPFTKEPDLGVASINYDLADLLARSTNAEGSL

MLKLEEIKKDAQVRGIVEGQVVRVVTVEQIGEHALTVYYKDSKGVLAERMLFRSDEMALELATVGRAWAFDADGGDFKLGLEAYRISQAALFDPMMAVNMANVDPLPHQISAVYEYMLPKQPLRYVLADDPGAGKTIMAGLFISELLLRADARRIMVVSPGSLTEQWQDELFEKFGLQFEIFSKEKQEQCATGNFFTETDRLICRLDQLSRSEELQEKLRNTDWDLIIVDEAHKLSANYFGNKINKTKRFALGELLGSICRHFLLMTATPHNGKEEDFQVWMSLLDSDRFYGKFREGAHKVDITDMMRRMVKEELLTFDGTPLFPERRAYTANYDLSSLEASLYEQVTTYVREEMNRADKLDNKKKNTVGFALTQLQRRLASSPEAIYQSLKRRRNRLKDKLAEMKLLARGQKAKLTGVAETLGSYTVTKQLDLPDNWDELDEDLSAEEYELYAEQVADQATAAETILELDAEILSLKDLEQQALLLVQSGNDKKWEQLSALLQDSPEMKNRDGSRRKLIIFTEHKDTLNYLRQRVGDLLGQSNAVRVIYGGTNRDERRKIQSEFRSDPTVLVLIATDAAGEGVNLQNANLMVNYDLPWNPNRLEQRFGRIHRIGQKEVCHLWNIVANETREGEVFQKLFAKLEIEKQALGGKVFDILGEAFDNVSLKQLLMDAIRYGEDPAVRARMDQAIEGALDSDHLKEIMRRNALVESHMGMEGLYAIKEQMEKAEARRLQPFFIRAFFQEAFQMLGGDLREREQGRYEIRHVPAVIRERDRTIGESRTPVLPRYERVCFEKQLTRPTGKVLAELLHPVHPLMHSVLDLTLQAHRGKLKQGAVLVDPADDCDEPRLIIMLEHSVRETAEQAKSIASRRLQFVAIDKACQASYAGWAPHLDLVPISEGDLTLVQDILCSPWLSQPLEPLALQLASEKLVPEHFAEVKTRRELQADKTLAAVHERLIKEINYWQDRYLKLSDDVKSGKQPRMQPENARRRVDELTARLQQRTTELTALKQVVSSTPVVIGSALVIPQGLLAKRKGEVMFSPDAASRAHIERVAMQAVTDAEQALGHMVIDVAADKCGWDITARPPLKSDGSLPQDRHIEVKGRSKGQITITVSRNEILYALNQADKFLLAIVLVEGDKAEGPYYIRQPFTKEPDLGVASINYDLADLLARSTNAEGSL

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

4 GO

Subcellular localization

Localization: Cytoplasmic

Gene Ontology (GO)

GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0140658 An activity, driven by ATP hydrolysis, that modulates the contacts between histones and DNA, resulting in a change in chromosome architecture within the nucleosomal array, leading to chromatin remodeling.
GO:0004386 Catalysis of the reaction: ATP + H2O = ADP + phosphate, to drive the unwinding of a DNA or RNA helix.
GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

28 records

Show feature table

Start	End	DB	Term	Name
993	1013	Coils	Coil	Coil
526	615	SMART	SM00490	helicmild6
526	615	InterPro	IPR001650	Helicase, C-terminal
124	369	Pfam	PF00176	SNF2-related domain
124	369	InterPro	IPR000330	SNF2, N-terminal
498	666	ProSiteProfiles	PS51194	Superfamilies 1 and 2 helicase C-terminal domain profile.
498	666	InterPro	IPR001650	Helicase, C-terminal
116	288	ProSiteProfiles	PS51192	Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile.
116	288	InterPro	IPR014001	Helicase superfamily 1/2, ATP-binding domain
95	291	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
95	291	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
105	309	CDD	cd18011	DEXDc_RapA
433	645	Gene3D	G3DSA:3.40.50.300	-
433	645	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
222	657	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
222	657	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
107	686	PANTHER	PTHR10799	SNF2/RAD54 HELICASE FAMILY
101	304	SMART	SM00487	ultradead3
101	304	InterPro	IPR014001	Helicase superfamily 1/2, ATP-binding domain
493	626	CDD	cd18793	SF2_C_SNF
1051	1143	Pfam	PF13020	Protein NO VEIN, C-terminal
1051	1143	InterPro	IPR024975	Protein NO VEIN, C-terminal
495	615	Pfam	PF00271	Helicase conserved C-terminal domain
495	615	InterPro	IPR001650	Helicase, C-terminal
1180	1180	Coils	Coil	Coil
388	415	Coils	Coil	Coil
102	423	Gene3D	G3DSA:3.40.50.10810	-
102	423	InterPro	IPR038718	SNF2-like, N-terminal domain superfamily

3D structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; AlphaFold DB and ColabFold models typically cover the full protein but remain computational predictions.

Download VMD script Full viewer

Loading 3D structure...

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

Pocket score High Medium Low

How colors and pocket overlays are used

Uniform protein color marks the displayed model as a single molecular object.

Experimental PDB structures may be colored by chain to distinguish subunits or copies present in the file.

Pocket colors and alpha spheres are evidence overlays for predicted binding cavities; they are not alternative protein chains.

'Alpha spheres' is FPocket's own cavity-shape geometry, imported when available and aligned with the loaded structure.

'Pocket atoms'/'Predicted site atoms' show the pocket's residue atoms instead: P2Rank reports residues rather than alpha spheres, and FPocket falls back to this when alpha-sphere geometry is unavailable or doesn't align.

'No pocket geometry' means neither alpha spheres nor residue-position data could be found for that pocket; the layer just highlights the same residues as 'Nearby residues'.

Pocket details Inspect a specific pocket, or open the full viewer

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.94

Show in viewer

Surrounding area

Pocket 2 P2Rank #2

0.825

Show in viewer

Surrounding area

Pocket 3 P2Rank #3

0.729

Show in viewer

Surrounding area

Pocket 4 P2Rank #4

0.451

Show in viewer

Surrounding area

Pocket 5 P2Rank #5

0.386

Likely same site as FPocket 22 3.1 Å 10 shared residues 77% of smaller site

Show in viewer

Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #22

0.883

Likely same site as P2Rank 5 3.1 Å 10 shared residues 77% of smaller site

Show in viewer

Surrounding area

Pocket 2 FPocket #2

0.75 Unusual size

Show in viewer

Surrounding area

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.986

Show in viewer

Surrounding area

Pocket 2 P2Rank #2

0.829

Show in viewer

Surrounding area

Pocket 3 P2Rank #3

0.803

Show in viewer

Surrounding area

Pocket 4 P2Rank #4

0.416

Show in viewer

Surrounding area

Pocket 5 P2Rank #5

0.388

Show in viewer

Surrounding area

All structural evidence 0 experimental · 2 predicted

Structural evidence

0 + 2

Experimental PDB entries plus predicted AlphaFold DB or ColabFold models. Click Switch to display a different loaded structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold DB AF_A0A6A8EMP7	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_01338	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.

57 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 7 records from similar proteins

Structural ligands 7 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

ANP PDB via homolog Detail RCSB PDB

BEF PDB via homolog Detail RCSB PDB

DC PDB via homolog Detail RCSB PDB

DG 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
AGS RCSB PDB	3MWY	P32657	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)…`
ANP RCSB PDB	6RYR	Q14839	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)…`
BEF RCSB PDB	5Z3U	P22082	66.0 Da LogP 0.88 TPSA 0.0	✓ Ro5	✓ Clean	`[Be-](F)(F)F`
DC RCSB PDB	6G0L	P32657	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`C1[C@@H]([C@H](O[C@H]1N2C=CC(=NC2=O)N)COP(=O)(O…`
DG RCSB PDB	6G0L	P32657	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	6G0L	P32657	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…`
KH2 RCSB PDB	5HZR	G2QDW1	221.3 Da LogP 0.55 TPSA 57.2	✓ Ro5	✓ Clean	`C[N+]1(CCCCC1)CCCS(=O)(=O)[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
ZINC12503923 ZINC	1.000	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@@H](O)[C@@H](COP(=O)(O)O)O2)c…`
ZINC12503924 ZINC	1.000	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2C[C@@H](O)[C@@H](COP(=O)(O)O)O2)c(…`
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(…`
ZINC1532581 ZINC	1.000	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@@H](O)[C@H](COP(=O)(O)O)O2)c(…`
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…`
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…`
ZINC3645374 ZINC	1.000	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@H](O)[C@@H](COP(=O)(O)O)O2)c(…`
ZINC3861759 ZINC	1.000	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2C[C@H](O)[C@@H](COP(=O)(O)O)O2)c(=…`
ZINC3869816 ZINC	1.000	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@H](O)[C@H](COP(=O)(O)O)O2)c(=…`
ZINC3869817 ZINC	1.000	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2C[C@H](O)[C@H](COP(=O)(O)O)O2)c(=O…`
ZINC3869818 ZINC	1.000	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2C[C@@H](O)[C@H](COP(=O)(O)O)O2)c(=…`
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)…`
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…`
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`
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…`
ZINC3983944 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)[…`
ZINC404254 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)[…`
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…`
ZINC404257 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)[nH…`
ZINC8613543 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)…`

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 A0A6A8EMP7