KpKP13 Protein target profile

L-lactate dehydrogenase 2

Accession: KP13_05264

Gene: ldh2 AHE44671.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GN55

Export view

Length 314

Pocket druggability (P2Rank · AlphaFold DB model) 0.859

Direct ligand evidence 0 60 total records

Functional annotation 1 EC 8 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 0.57. This supports review but is not experimental validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.86. 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 (%): 34.359 Lower values reduce human off-target concern.
Human E-value: 2.64e-36
Gut microbiome similarity: 0.5% 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: 95.07 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) 0.859

Structure A0A0H3GN55

Pocket Pocket 1

Druggability (FPocket) 0.568

Structure A0A0H3GN55

Pocket Pocket 15

ColabFold model

P2Rank 0.893 · Pocket 1

FPocket 0.455 · Pocket 14

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 26 / 4744 genomes with a hit

Prevalence 0.5%

Sequence

Primary amino-acid sequence viewer.

MHTKARKVMIIGAGNVGASAAYALLNQSICEELILVDLNQQRAEAHAQDLSDAAAYLPGMMTISTREASDCADVDIAVITVSGGALRPGQSRLDELTSTAKIVKSIVPTMMANGFNGIFLVATNPCDIITWQVWQLSGLPRSQVLGTGVWLDTTRLRRLLAQELEIGAQSIDAFILGEHGDTQFPVWSHSSVYGTPIADLYQQRTGLPLDREAMADKVRKLGFEIYAGKGCTEYGVAGTIAEICRNIFTGSHRALAVSCILDGEYGVSGAAAGVPAVLAQGGVKQIIELQLAGEEQAKFSQSIAVIKANIARLP

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

1.1.1.27

Gene Ontology (GO)

GO:0016616 Catalysis of an oxidation-reduction (redox) reaction in which a CH-OH group acts as a hydrogen or electron donor and reduces NAD+ or NADP.
GO:0019752 The chemical reactions and pathways involving carboxylic acids, any organic acid containing one or more carboxyl (COOH) groups or anions (COO-).
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0004459 Catalysis of the reaction: (S)-lactate + NAD+ = pyruvate + NADH + H+.
GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
GO:0006096 The chemical reactions and pathways resulting in the breakdown of a carbohydrate into pyruvate, with the concomitant production of a small amount of ATP and the reduction of NAD(P) to NAD(P)H. Glycolysis begins with the metabolism of a carbohydrate to generate products that can enter the pathway and ends with the production of pyruvate. Pyruvate may be converted to acetyl-coenzyme A, ethanol, lactate, or other small molecules.
GO:0006089 The chemical reactions and pathways involving lactate, the anion of lactic acid.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

31 records

Show feature table

Start	End	DB	Term	Name
2	313	PIRSF	PIRSF000102	Lac_mal_DH
2	313	InterPro	IPR001557	L-lactate/malate dehydrogenase
150	313	Gene3D	G3DSA:3.90.110.10	-
150	313	InterPro	IPR015955	Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal
4	310	PANTHER	PTHR43128	L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+))
5	314	Hamap	MF_00488	L-lactate dehydrogenase [ldh].
5	314	InterPro	IPR011304	L-lactate dehydrogenase
10	307	NCBIfam	TIGR01771	L-lactate dehydrogenase
10	307	InterPro	IPR011304	L-lactate dehydrogenase
1	148	Gene3D	G3DSA:3.40.50.720	-
176	182	ProSitePatterns	PS00064	L-lactate dehydrogenase active site.
176	182	InterPro	IPR018177	L-lactate dehydrogenase, active site
6	312	CDD	cd05291	HicDH_like
3	146	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
3	146	InterPro	IPR036291	NAD(P)-binding domain superfamily
7	146	Pfam	PF00056	lactate/malate dehydrogenase, NAD binding domain
7	146	InterPro	IPR001236	Lactate/malate dehydrogenase, N-terminal
151	311	Pfam	PF02866	lactate/malate dehydrogenase, alpha/beta C-terminal domain
151	311	InterPro	IPR022383	Lactate/malate dehydrogenase, C-terminal
144	162	PRINTS	PR00086	L-lactate dehydrogenase signature
144	162	InterPro	IPR001557	L-lactate/malate dehydrogenase
174	187	PRINTS	PR00086	L-lactate dehydrogenase signature
174	187	InterPro	IPR001557	L-lactate/malate dehydrogenase
120	140	PRINTS	PR00086	L-lactate dehydrogenase signature
120	140	InterPro	IPR001557	L-lactate/malate dehydrogenase
32	56	PRINTS	PR00086	L-lactate dehydrogenase signature
32	56	InterPro	IPR001557	L-lactate/malate dehydrogenase
7	31	PRINTS	PR00086	L-lactate dehydrogenase signature
7	31	InterPro	IPR001557	L-lactate/malate dehydrogenase
147	311	SUPERFAMILY	SSF56327	LDH C-terminal domain-like
147	311	InterPro	IPR015955	Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal

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

0.859

Likely same site as FPocket 15 3.0 Å 26 shared residues 100% of smaller site

Show in viewer

Surrounding area

Pocket 2 P2Rank #2

0.128

Show in viewer

Surrounding area

Pocket 3 P2Rank #3

0.02

Show in viewer

Surrounding area

Pocket 4 P2Rank #4

0.018

Likely same site as FPocket 16 2.4 Å 10 shared residues 100% of smaller site

Show in viewer

Surrounding area

Pocket 5 P2Rank #5

0.01

Likely same site as FPocket 16 3.2 Å 8 shared residues 100% 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 #15

0.568 Unusual size

Likely same site as P2Rank 1 3.0 Å 26 shared residues 100% of smaller site

Show in viewer

Surrounding area

Pocket 2 FPocket #16

0.308

Likely same site as P2Rank 4 2.4 Å 10 shared residues 100% of smaller site

Show in viewer

Surrounding area

Residue sets

UniProt: Active site:179-179 Proton acceptor

UniProt: Binding site:105-105

UniProt: Binding site:12-17

UniProt: Binding site:122-124

UniProt: Binding site:124-127

UniProt: Binding site:147-147

UniProt: Binding site:152-155

UniProt: Binding site:16-16

UniProt: Binding site:232-232

UniProt: Binding site:37-37

UniProt: Binding site:42-42

UniProt: Binding site:92-92

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.893

Show in viewer

Surrounding area

Pocket 2 P2Rank #2

0.106

Show in viewer

Surrounding area

Pocket 3 P2Rank #3

0.02

Likely same site as FPocket 14 2.2 Å 11 shared residues 100% of smaller site

Show in viewer

Surrounding area

Pocket 4 P2Rank #4

0.019

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_A0A0H3GN55	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_05264	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.

60 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 10 records from similar proteins

Structural ligands 10 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

1E4 PDB via homolog 748.1 Da · LogP 2.97 · TPSA 238.1 Open detail RCSB PDB

1E5 PDB via homolog Detail RCSB PDB

1E6 PDB via homolog Detail RCSB PDB

1E7 PDB via homolog Detail RCSB PDB

6P3 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
1E4 RCSB PDB	4I9H	P13491	748.1 Da LogP 2.97 TPSA 238.1	3 viol.	✓ Clean	`COc1cc(c(cc1NC(=O)CSc2ccc(cn2)C(=O)O)Cl)OC[C@H]…`
1E5 RCSB PDB	4I9N	P13491	291.2 Da LogP 2.05 TPSA 96.7	✓ Ro5	✓ Clean	`c1cc(ncc1C(=O)O)c2cc(cc(c2)F)OCC(=O)O`
1E6 RCSB PDB	4I9N	P13491	442.9 Da LogP 1.90 TPSA 138.2	✓ Ro5	✓ Clean	`COc1cc(c(cc1NC(=O)CSc2ccc(cn2)C(=O)O)Cl)OC[C@H]…`
1E7 RCSB PDB	4I9U	P13491	352.8 Da LogP 3.17 TPSA 88.5	✓ Ro5	✓ Clean	`COc1ccc(cc1NC(=O)CSc2ccc(cn2)C(=O)O)Cl`
6P3 RCSB PDB	4I8X	P13491	199.2 Da LogP 2.45 TPSA 50.2	✓ Ro5	✓ Clean	`c1ccc(cc1)c2ccc(cn2)C(=O)O`
6V0 RCSB PDB	5KKC	P13491	665.4 Da LogP -3.03 TPSA 317.6	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
APR RCSB PDB	7BYA	A0A143T1U9	559.3 Da LogP -3.28 TPSA 291.5	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
MLI RCSB PDB	5NQB	P13491	102.0 Da LogP -3.12 TPSA 80.3	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(=O)[O-]`
OAA RCSB PDB	7BY9	A0A143T1U9	131.1 Da LogP -2.22 TPSA 94.5	✓ Ro5	✓ Clean	`C(C(=O)C(=O)O)C(=O)[O-]`
PYR RCSB PDB	6J9U	P00343	88.1 Da LogP -0.34 TPSA 54.4	✓ Ro5	✓ Clean	`CC(=O)C(=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
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(=…`
ZINC65347758 ZINC	0.815	243.2 Da LogP 2.15 TPSA 87.5	✓ Ro5	✓ Clean	`O=C(O)c1ccc(-c2ccc(C(=O)O)cn2)cc1`
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…`
ZINC6811580 ZINC	0.755	336.8 Da LogP 3.47 TPSA 79.3	✓ Ro5	✓ Clean	`Cc1ccc(Cl)cc1NC(=O)CSc1ccc(C(=O)O)cn1`
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](…`
ZINC20442012 ZINC	0.742	200.2 Da LogP 1.84 TPSA 63.1	✓ Ro5	✓ Clean	`O=C(O)c1ccc(-c2cccnc2)nc1`
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)…`
ZINC39927691 ZINC	0.733	213.2 Da LogP 2.76 TPSA 50.2	✓ Ro5	✓ Clean	`Cc1ccc(-c2ccc(C(=O)O)cn2)cc1`
ZINC47214424 ZINC	0.733	200.2 Da LogP 1.84 TPSA 63.1	✓ Ro5	✓ Clean	`O=C(O)c1ccc(-c2ccncc2)nc1`
ZINC65347120 ZINC	0.733	215.2 Da LogP 2.15 TPSA 70.4	✓ Ro5	✓ Clean	`O=C(O)c1ccc(-c2ccc(O)cc2)nc1`
ZINC5017776 ZINC	0.731	244.2 Da LogP 1.54 TPSA 100.4	✓ Ro5	✓ Clean	`O=C(O)c1ccc(-c2ccc(C(=O)O)cn2)nc1`
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…`
ZINC65347600 ZINC	0.718	235.2 Da LogP 2.73 TPSA 50.2	✓ Ro5	✓ Clean	`O=C(O)c1ccc(-c2cc(F)cc(F)c2)nc1`
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@…`

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 A0A0H3GN55