KpKP13 Protein target profile

Glucose-1-phosphate adenylyltransferase

Accession: KP13_00665

Gene: AHE42284.1 glgC 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GZJ7

Export view

Length 431

Pocket druggability (P2Rank · AlphaFold DB model) 0.941

Direct ligand evidence 0 81 total records

Functional annotation 1 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

Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Moderate predicted binding pocket FPocket selected-pocket score 0.45. This supports review but is not experimental 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 (%): 27.841 Lower values reduce human off-target concern.
Human E-value: 5.25e-06
Gut microbiome similarity: 3.6% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 44.612 Higher values support similarity to known essential genes.
DEG E-value: 9.94e-122 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 93.36 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) 0.941

Structure A0A0H3GZJ7

Pocket Pocket 1

Druggability (FPocket) 0.446

Structure A0A0H3GZJ7

Pocket Pocket 5

ColabFold model

P2Rank 0.937 · Pocket 1

FPocket 0.419 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 171 / 4744 genomes with a hit

Prevalence 3.6%

Sequence

Primary amino-acid sequence viewer.

MVRLEKNDPLMLARQLPIKSVALILAGGRGTRLKDLTIKRAKPAVHFGGKFRIIDFALSNCINSGIRRIGVITQYQSHTLVQHIQRGWSFFSEEMNEFVDLLPAQQRVHGENWYRGTADAVTQNLDIISRYKAEYVVILAGDHIYKQDYSRMLIDHVEKGARCTVACMPVPIEEASAFGVMAVDENEKIIEFVEKPANPPAMPTDPTKSLASMGIYVFDAAYLYELLEEDDRNENSSHDFGKDIIPKITEAGMAYAHPFPLSCVQSDPNAEPYWRDVGTLEAYWKANLDLASVTPELDMYDQNWPIRTHMESLPPAKFVQDRSGSHGMTLNSLVSGGCIISGSVVVQSVLFPRVRVNSFCNIDSAVLLPDVWVGRSCRLRRCVIDRACVIPEGMVIGENAEEDARRFYRSEEGIVLVTRDMLRKLGHKQER

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 4 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

2.7.7.27

Gene Ontology (GO)

GO:0009058 A cellular process consisting of the biochemical pathways by which a living organism synthesizes chemical substances. This typically represents the energy-requiring part of metabolism in which simpler substances are transformed into more complex ones.
GO:0005978 The chemical reactions and pathways resulting in the formation of glycogen, a polydisperse, highly branched glucan composed of chains of D-glucose residues.
GO:0008878 Catalysis of the reaction: alpha-D-glucose 1-phosphate + ATP = ADP-glucose + diphosphate.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

23 records

Show feature table

Start	End	DB	Term	Name
26	45	ProSitePatterns	PS00808	ADP-glucose pyrophosphorylase signature 1.
26	45	InterPro	IPR005836	ADP-glucose pyrophosphorylase, conserved site
301	431	FunFam	G3DSA:2.160.10.10:FF:000006	Glucose-1-phosphate adenylyltransferase
1	300	Gene3D	G3DSA:3.90.550.10	Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A
1	300	InterPro	IPR029044	Nucleotide-diphospho-sugar transferases
321	422	CDD	cd04651	LbH_G1P_AT_C
17	423	Hamap	MF_00624	Glucose-1-phosphate adenylyltransferase [glgC].
17	423	InterPro	IPR023049	Glucose-1-phosphate adenylyltransferase GlgC, bacterial
14	422	PANTHER	PTHR43523	GLUCOSE-1-PHOSPHATE ADENYLYLTRANSFERASE-RELATED
14	422	InterPro	IPR011831	Glucose-1-phosphate adenylyltransferase
22	291	Pfam	PF00483	Nucleotidyl transferase
22	291	InterPro	IPR005835	Nucleotidyl transferase domain
22	277	CDD	cd02508	ADP_Glucose_PP
113	121	ProSitePatterns	PS00809	ADP-glucose pyrophosphorylase signature 2.
113	121	InterPro	IPR005836	ADP-glucose pyrophosphorylase, conserved site
20	393	SUPERFAMILY	SSF53448	Nucleotide-diphospho-sugar transferases
20	393	InterPro	IPR029044	Nucleotide-diphospho-sugar transferases
312	411	SUPERFAMILY	SSF51161	Trimeric LpxA-like enzymes
312	411	InterPro	IPR011004	Trimeric LpxA-like superfamily
1	300	FunFam	G3DSA:3.90.550.10:FF:000014	Glucose-1-phosphate adenylyltransferase
21	397	NCBIfam	TIGR02091	glucose-1-phosphate adenylyltransferase
21	397	InterPro	IPR011831	Glucose-1-phosphate adenylyltransferase
301	431	Gene3D	G3DSA:2.160.10.10	Hexapeptide repeat proteins

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

0.941

Show in viewer

Surrounding area

Pocket 2 P2Rank #2

0.52

Show in viewer

Surrounding area

Pocket 3 P2Rank #3

0.103

Show in viewer

Surrounding area

Pocket 4 P2Rank #4

0.034

Show in viewer

Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #5

0.446 Unusual size

Show in viewer

Surrounding area

Residue sets

UniProt: Binding site:114-114

UniProt: Binding site:130-130

UniProt: Binding site:179-179

UniProt: Binding site:194-195

UniProt: Binding site:212-212

UniProt: Binding site:370-370

UniProt: Binding site:386-386

UniProt: Binding site:39-39

UniProt: Binding site:40-40

UniProt: Binding site:419-423

UniProt: Binding site:46-46

UniProt: Binding site:52-52

UniProt: Site:113-113 Could play a key role in the communication between the regulatory and the substrate sites

UniProt: Site:74-74 Could play a key role in the communication between the regulatory and the substrate sites

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.937

Show in viewer

Surrounding area

Pocket 2 P2Rank #2

0.56

Show in viewer

Surrounding area

Pocket 3 P2Rank #3

0.077

Show in viewer

Surrounding area

Pocket 4 P2Rank #4

0.033

Show in viewer

Surrounding area

Pocket 5 P2Rank #5

0.006

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_A0A0H3GZJ7	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_00665	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.

81 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 31 records from similar proteins

Structural ligands 31 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

4WF PDB via homolog 233.2 Da · LogP -0.13 · TPSA 101.1 Open detail RCSB PDB

942 PDB via homolog Detail RCSB PDB

9X7 PDB via homolog Detail RCSB PDB

ADQ PDB via homolog Detail RCSB PDB

BBE 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
4WF RCSB PDB	3ZLL	Q9HU22	233.2 Da LogP -0.13 TPSA 101.1	✓ Ro5	✓ Clean	`c1ccc(cc1)CN2C(=C(C(=O)NC2=O)N)O`
942 RCSB PDB	4B42	Q9HU22	316.4 Da LogP 1.20 TPSA 101.2	✓ Ro5	✓ Clean	`CCCCN1C(=C(C(=O)NC1=O)N(C)C(=O)c2ccccc2)N`
9X7 RCSB PDB	5W5T	P39669	116.1 Da LogP 0.14 TPSA 43.4	✓ Ro5	✓ Clean	`CCOC(=O)C(=O)C`
ADQ RCSB PDB	1YP4	P23509	589.3 Da LogP -3.92 TPSA 311.7	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
BBE RCSB PDB	4B5B	Q9HU22	400.5 Da LogP 1.30 TPSA 118.3	✓ Ro5	✓ Clean	`Cc1cccc(c1)S(=O)(=O)N(C)C2=C(N(C(=O)NC2=O)Cc3cc…`
BZ0 RCSB PDB	4B2W	Q9HU22	336.4 Da LogP 1.42 TPSA 110.0	✓ Ro5	✓ Clean	`c1ccc(cc1)CN2C(=C(C(=O)NC2=O)NC(=O)c3ccccc3)N`
DAU RCSB PDB	4ECM	A0A6L8PCC3	564.3 Da LogP -3.46 TPSA 276.8	3 viol.	✓ Clean	`CC1=CN(C(=O)NC1=O)[C@H]2C[C@@H]([C@H](O2)CO[P@]…`
DH5 RCSB PDB	5FU8	Q9HU22	479.4 Da LogP 2.06 TPSA 118.3	✓ Ro5	✓ Clean	`Cc1cc(ccc1Br)CN2C(=C(C(=O)NC2=O)N(C)S(=O)(=O)c3…`
FKH RCSB PDB	5FU0	Q9HU22	400.5 Da LogP 1.30 TPSA 118.3	✓ Ro5	✓ Clean	`Cc1cccc(c1)CN2C(=C(C(=O)NC2=O)N(C)S(=O)(=O)c3cc…`
GJB RCSB PDB	4B4B	Q9HU22	232.2 Da LogP 0.70 TPSA 66.5	✓ Ro5	✓ Clean	`c1ccc(cc1)CCN2C(=O)CC(=O)NC2=O`
GNH RCSB PDB	6JQ8	Q8GJ95	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…`
HKX RCSB PDB	5FUH	Q9HU22	465.3 Da LogP 1.75 TPSA 118.3	✓ Ro5	✓ Clean	`CN(C1=C(N(C(=O)NC1=O)Cc2cccc(c2)Br)N)S(=O)(=O)c…`
HNR RCSB PDB	4ARW	Q9HU22	352.4 Da LogP 0.74 TPSA 118.3	✓ Ro5	✓ Clean	`CCCCN1C(=C(C(=O)NC1=O)N(C)S(=O)(=O)c2ccccc2)N`
JWT RCSB PDB	4B4M	Q9HU22	404.4 Da LogP 1.13 TPSA 118.3	✓ Ro5	✓ Clean	`CN(C1=C(N(C(=O)NC1=O)Cc2ccccc2)N)S(=O)(=O)c3ccc…`
KDT RCSB PDB	5FTV	Q9HU22	465.3 Da LogP 1.75 TPSA 118.3	✓ Ro5	✓ Clean	`CN(C1=C(N(C(=O)NC1=O)Cc2ccc(cc2)Br)N)S(=O)(=O)c…`
KKT RCSB PDB	4B4G	Q9HU22	366.4 Da LogP 0.73 TPSA 118.3	✓ Ro5	✓ Clean	`CCCCS(=O)(=O)N(C)C1=C(N(C(=O)NC1=O)Cc2ccccc2)N`
LD6 RCSB PDB	5FYE	Q9HU22	404.4 Da LogP 1.13 TPSA 118.3	✓ Ro5	✓ Clean	`CN(C1=C(N(C(=O)NC1=O)Cc2cccc(c2)F)N)S(=O)(=O)c3…`
M9Z RCSB PDB	6T37	Q9HU22	524.6 Da LogP 0.96 TPSA 161.0	1 viol.	✓ Clean	`CN(C1=C(N(C(=O)NC1=O)Cc2ccccc2)NCCCn3cc(nn3)CN)…`
MBK RCSB PDB	6T38	Q9HU22	536.5 Da LogP 2.32 TPSA 130.3	1 viol.	✓ Clean	`CN(C1=C(N(C(=O)NC1=O)Cc2ccc(cc2)Br)NCCCCN)S(=O)…`
N5Y RCSB PDB	4ASY	Q9HU22	350.4 Da LogP 1.44 TPSA 101.2	✓ Ro5	✓ Clean	`CN(C1=C(N(C(=O)NC1=O)Cc2ccccc2)N)C(=O)c3ccccc3`
N6A RCSB PDB	4ASJ	Q9HU22	386.4 Da LogP 0.99 TPSA 118.3	✓ Ro5	✓ Clean	`CN(C1=C(N(C(=O)NC1=O)Cc2ccccc2)N)S(=O)(=O)c3ccc…`
NIQ RCSB PDB	4B2X	Q9HU22	266.3 Da LogP 1.27 TPSA 92.9	✓ Ro5	✓ Clean	`CCCCN1C(=C(C(=O)NC1=O)NC2CCCC2)N`
NVQ RCSB PDB	6TQG	Q9HU22	536.5 Da LogP 2.19 TPSA 116.3	1 viol.	✓ Clean	`CNCCCNC1=C(C(=O)NC(=O)N1Cc2ccc(cc2)Br)N(C)S(=O)…`
NWL RCSB PDB	4B3U	Q9HU22	260.3 Da LogP 0.60 TPSA 92.9	✓ Ro5	✓ Clean	`CCNC1=C(N(C(=O)NC1=O)Cc2ccccc2)N`
P3I RCSB PDB	5FTS	Q9HU22	465.3 Da LogP 1.75 TPSA 118.3	✓ Ro5	✓ Clean	`CN(C1=C(N(C(=O)NC1=O)Cc2ccccc2Br)N)S(=O)(=O)c3c…`
PMB RCSB PDB	1YP2	P23509	357.8 Da LogP 0.11 TPSA 54.4	✓ Ro5	✓ Clean	`c1cc(ccc1S(=O)(=O)O)[Hg]`
POP RCSB PDB	4ECM	A0A6L8PCC3	176.0 Da LogP -2.08 TPSA 129.9	✓ Ro5	✓ Clean	`O[P@@](=O)([O-])O[P@@](=O)(O)[O-]`
PYR RCSB PDB	5W5R	P39669	88.1 Da LogP -0.34 TPSA 54.4	✓ Ro5	✓ Clean	`CC(=O)C(=O)O`
TRH RCSB PDB	1G3L	Q9HU22	548.3 Da LogP -2.43 TPSA 256.5	3 viol.	✓ Clean	`C[C@H]1[C@@H]([C@H]([C@H]([C@H](O1)O[P@](=O)(O)…`
TTP RCSB PDB	1G2V	Q9HU22	482.2 Da LogP -1.16 TPSA 244.1	2 viol.	✓ Clean	`CC1=CN(C(=O)NC1=O)[C@H]2C[C@@H]([C@H](O2)CO[P@]…`
Y46 RCSB PDB	3ZLK	Q9HU22	372.4 Da LogP 0.97 TPSA 127.0	✓ Ro5	✓ Clean	`c1ccc(cc1)CN2C(=C(C(=O)NC2=O)NS(=O)(=O)c3ccccc3…`

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
ZINC14140848 ZINC	1.000	352.4 Da LogP 0.74 TPSA 118.3	✓ Ro5	✓ Clean	`CCCCn1c(N)c(N(C)S(=O)(=O)c2ccccc2)c(=O)[nH]c1=O`
ZINC17083504 ZINC	1.000	233.2 Da LogP -0.13 TPSA 101.1	✓ Ro5	✓ Clean	`Nc1c(O)n(Cc2ccccc2)c(=O)[nH]c1=O`
ZINC3246457 ZINC	1.000	266.3 Da LogP 1.27 TPSA 92.9	✓ Ro5	✓ Clean	`CCCCn1c(N)c(NC2CCCC2)c(=O)[nH]c1=O`
ZINC3276805 ZINC	1.000	260.3 Da LogP 0.60 TPSA 92.9	✓ Ro5	✓ Clean	`CCNc1c(N)n(Cc2ccccc2)c(=O)[nH]c1=O`
ZINC4344385 ZINC	1.000	232.2 Da LogP 0.70 TPSA 66.5	✓ Ro5	✓ Clean	`O=C1CC(=O)N(CCc2ccccc2)C(=O)N1`
ZINC7688373 ZINC	1.000	350.4 Da LogP 1.44 TPSA 101.2	✓ Ro5	✓ Clean	`CN(C(=O)c1ccccc1)c1c(N)n(Cc2ccccc2)c(=O)[nH]c1=O`
ZINC7799558 ZINC	1.000	316.4 Da LogP 1.20 TPSA 101.2	✓ Ro5	✓ Clean	`CCCCn1c(N)c(N(C)C(=O)c2ccccc2)c(=O)[nH]c1=O`
ZINC104869865 ZINC	0.879	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	0.879	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	0.879	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	0.879	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	0.879	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	0.879	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	0.879	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)(…`
ZINC6552309 ZINC	0.844	378.4 Da LogP 2.01 TPSA 101.2	✓ Ro5	✓ Clean	`CCc1ccc(C(=O)N(C)c2c(N)n(Cc3ccccc3)c(=O)[nH]c2=…`
ZINC7799574 ZINC	0.809	330.4 Da LogP 1.50 TPSA 101.2	✓ Ro5	✓ Clean	`CCCCn1c(N)c(N(C)C(=O)c2ccc(C)cc2)c(=O)[nH]c1=O`
ZINC9245373 ZINC	0.809	428.5 Da LogP 0.85 TPSA 135.3	✓ Ro5	✓ Clean	`CN(C(=O)c1ccc(S(C)(=O)=O)cc1)c1c(N)n(Cc2ccccc2)…`
ZINC3269772 ZINC	0.805	274.3 Da LogP 0.99 TPSA 92.9	✓ Ro5	✓ Clean	`CCCNc1c(N)n(Cc2ccccc2)c(=O)[nH]c1=O`
ZINC5861124 ZINC	0.792	395.4 Da LogP 1.35 TPSA 144.3	✓ Ro5	✓ Clean	`CN(C(=O)c1ccc([N+](=O)[O-])cc1)c1c(N)n(Cc2ccccc…`
ZINC7764539 ZINC	0.792	330.4 Da LogP 1.59 TPSA 101.2	✓ Ro5	✓ Clean	`CCCCn1c(N)c(N(CC)C(=O)c2ccccc2)c(=O)[nH]c1=O`
ZINC7799530 ZINC	0.792	395.3 Da LogP 1.96 TPSA 101.2	✓ Ro5	✓ Clean	`CCCCn1c(N)c(N(C)C(=O)c2ccc(Br)cc2)c(=O)[nH]c1=O`
ZINC7799632 ZINC	0.792	344.4 Da LogP 1.76 TPSA 101.2	✓ Ro5	✓ Clean	`CCCCn1c(N)c(N(C)C(=O)c2ccc(CC)cc2)c(=O)[nH]c1=O`
ZINC8704564 ZINC	0.792	317.3 Da LogP 0.59 TPSA 114.1	✓ Ro5	✓ Clean	`CCCCn1c(N)c(N(C)C(=O)c2ccncc2)c(=O)[nH]c1=O`
ZINC14656277 ZINC	0.776	372.5 Da LogP 2.49 TPSA 101.2	✓ Ro5	✓ Clean	`CCCCn1c(N)c(N(C)C(=O)c2ccc(C(C)(C)C)cc2)c(=O)[n…`
ZINC9463446 ZINC	0.776	443.5 Da LogP 2.85 TPSA 106.1	✓ Ro5	Alert	`Cc1ccc(C)n1-c1ccc(C(=O)N(C)c2c(N)n(Cc3ccccc3)c(…`
ZINC3226347 ZINC	0.775	322.4 Da LogP 1.78 TPSA 92.9	✓ Ro5	✓ Clean	`Nc1c(NCc2ccccc2)c(=O)[nH]c(=O)n1Cc1ccccc1`
ZINC339576 ZINC	0.767	288.3 Da LogP 0.15 TPSA 101.2	✓ Ro5	✓ Clean	`CC(=O)N(C)c1c(N)n(Cc2ccccc2)c(=O)[nH]c1=O`
ZINC3885656 ZINC	0.767	288.4 Da LogP 1.38 TPSA 92.9	✓ Ro5	✓ Clean	`CCCCNc1c(N)n(Cc2ccccc2)c(=O)[nH]c1=O`
ZINC14227155 ZINC	0.765	442.3 Da LogP 1.80 TPSA 101.2	✓ Ro5	✓ Clean	`CCCCn1c(N)c(N(C)C(=O)c2cccc(I)c2)c(=O)[nH]c1=O`
ZINC7799617 ZINC	0.765	334.4 Da LogP 1.33 TPSA 101.2	✓ Ro5	✓ Clean	`CCCCn1c(N)c(N(C)C(=O)c2cccc(F)c2)c(=O)[nH]c1=O`
ZINC8724791 ZINC	0.765	359.4 Da LogP 1.26 TPSA 104.4	✓ Ro5	✓ Clean	`CCCCn1c(N)c(N(C)C(=O)c2cccc(N(C)C)c2)c(=O)[nH]c…`
ZINC9450513 ZINC	0.765	350.8 Da LogP 1.85 TPSA 101.2	✓ Ro5	✓ Clean	`CCCCn1c(N)c(N(C)C(=O)c2cccc(Cl)c2)c(=O)[nH]c1=O`
ZINC8429382 ZINC	0.761	317.3 Da LogP 0.33 TPSA 113.2	✓ Ro5	✓ Clean	`CCNC(=O)N(C)c1c(N)n(Cc2ccccc2)c(=O)[nH]c1=O`
ZINC13120873 ZINC	0.760	442.5 Da LogP 3.24 TPSA 110.4	✓ Ro5	✓ Clean	`CN(C(=O)c1cccc(Oc2ccccc2)c1)c1c(N)n(Cc2ccccc2)c…`
ZINC14656013 ZINC	0.760	394.5 Da LogP 0.60 TPSA 135.3	✓ Ro5	✓ Clean	`CCCCn1c(N)c(N(C)C(=O)c2ccc(S(C)(=O)=O)cc2)c(=O)…`
ZINC8849862 ZINC	0.760	373.4 Da LogP 1.15 TPSA 130.3	✓ Ro5	✓ Clean	`CCCCn1c(N)c(N(C)C(=O)c2ccc(NC(C)=O)cc2)c(=O)[nH…`
ZINC9254063 ZINC	0.755	475.5 Da LogP 0.59 TPSA 138.6	✓ Ro5	✓ Clean	`CN(C(=O)CN(C)S(=O)(=O)c1ccc(F)cc1)c1c(N)n(Cc2cc…`
ZINC134152 ZINC	0.750	246.3 Da LogP 0.21 TPSA 92.9	✓ Ro5	✓ Clean	`CNc1c(N)n(Cc2ccccc2)c(=O)[nH]c1=O`
ZINC13519271 ZINC	0.750	466.2 Da LogP -0.13 TPSA 223.9	✓ Ro5	✓ Clean	`Cc1cn([C@H]2CC[C@@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC13546289 ZINC	0.750	466.2 Da LogP -0.13 TPSA 223.9	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2CC[C@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC7799609 ZINC	0.750	344.4 Da LogP 1.81 TPSA 101.2	✓ Ro5	✓ Clean	`CCCCn1c(N)c(N(C)C(=O)c2cc(C)cc(C)c2)c(=O)[nH]c1…`
ZINC14067326 ZINC	0.745	428.5 Da LogP 0.85 TPSA 135.3	✓ Ro5	✓ Clean	`CN(C(=O)c1cccc(S(C)(=O)=O)c1)c1c(N)n(Cc2ccccc2)…`
ZINC7799594 ZINC	0.745	341.4 Da LogP 1.07 TPSA 125.0	✓ Ro5	✓ Clean	`CCCCn1c(N)c(N(C)C(=O)c2ccc(C#N)cc2)c(=O)[nH]c1=O`
ZINC7988884 ZINC	0.745	407.4 Da LogP 1.40 TPSA 130.3	✓ Ro5	✓ Clean	`CC(=O)Nc1cccc(C(=O)N(C)c2c(N)n(Cc3ccccc3)c(=O)[…`
ZINC3269758 ZINC	0.744	288.4 Da LogP 1.24 TPSA 92.9	✓ Ro5	✓ Clean	`CC(C)CNc1c(N)n(Cc2ccccc2)c(=O)[nH]c1=O`
ZINC17107637 ZINC	0.741	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	0.741	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	0.741	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	0.741	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(=…`
ZINC5900144 ZINC	0.738	336.4 Da LogP 1.82 TPSA 92.9	✓ Ro5	✓ Clean	`Nc1c(NCCc2ccccc2)c(=O)[nH]c(=O)n1Cc1ccccc1`

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 A0A0H3GZJ7