KpATCC43816 Protein target profile

putative 2Fe-2S cluster-containing protein

Accession: VK055_1512

Gene: AIK80131.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A0H3GV44

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Length 369

Pocket druggability (P2Rank · AlphaFold DB model) 0.859

Direct ligand evidence 0 61 total records

Functional annotation 0 EC 5 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 0.42. 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 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: Hit
Human identity (%): 45.161 Lower values reduce human off-target concern.
Human E-value: 1.36e-19
Gut microbiome similarity: 2.3% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 40.58 Higher values support similarity to known essential genes.

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) 0.859

Structure A0A0H3GV44

Pocket Pocket 1

Druggability (FPocket) 0.417

Structure A0A0H3GV44

Pocket Pocket 13

ColabFold model

P2Rank 0.749 · Pocket 1

FPocket 0.807 · Pocket 4

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 107 / 4744 genomes with a hit

Prevalence 2.3%

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.

MVTLSRLFIHPVKSMRGMGLTHAFADISGLAFDRLFMVTETDGTFITARQFPQMVKFIPAPLHDGLHLTAPDGSSAVVRFSDFATQAEPTEVWGNHFTALIAPAAVNQWLSGFFKRDVQLRWLGPQLTRRVKRHDAVPLSFADGYPYLLANEASLRDLQQRCPASVSIEQFRPNLVVTGAAAWDEDSWKVIRIGEVVFDVAKPCSRCIFTTVSPERGQKHPAGEPLETLKRFRTALDNGDVDFGQNLIARNSGVIRVGDEVEILTRGPAKAYGAGESDDTPAPEAQQQATVAIEWQGQQFTGNNQQVLLEQLEQQGIRVPYSCRAGICGSCRIRLEEGEVSPLKKNAVAGDGTILACSCVPKTALRLAP

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

5 GO

Subcellular localization

Localization: Unknown

Gene Ontology (GO)

GO:0051537 Binding to a 2 iron, 2 sulfur (2Fe-2S) cluster; this cluster consists of two iron atoms, with two inorganic sulfur atoms found between the irons and acting as bridging ligands.
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:0030151 Binding to a molybdenum ion (Mo).
GO:0051536 Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms.
GO:0030170 Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

22 records

Show feature table

Start	End	DB	Term	Name
4	132	SUPERFAMILY	SSF141673	MOSC N-terminal domain-like
139	262	Pfam	PF03473	MOSC domain
139	262	InterPro	IPR005302	Molybdenum cofactor sulfurase, C-terminal
296	362	Pfam	PF00111	2Fe-2S iron-sulfur cluster binding domain
296	362	InterPro	IPR001041	2Fe-2S ferredoxin-type iron-sulfur binding domain
290	367	CDD	cd00207	fer2
290	367	InterPro	IPR001041	2Fe-2S ferredoxin-type iron-sulfur binding domain
1	116	Pfam	PF03476	MOSC N-terminal beta barrel domain
1	116	InterPro	IPR005303	Molybdenum cofactor sulfurase, middle domain
280	367	SUPERFAMILY	SSF54292	2Fe-2S ferredoxin-like
280	367	InterPro	IPR036010	2Fe-2S ferredoxin-like superfamily
115	264	ProSiteProfiles	PS51340	MOSC domain profile.
115	264	InterPro	IPR005302	Molybdenum cofactor sulfurase, C-terminal
287	369	ProSiteProfiles	PS51085	2Fe-2S ferredoxin-type iron-sulfur binding domain profile.
287	369	InterPro	IPR001041	2Fe-2S ferredoxin-type iron-sulfur binding domain
323	331	ProSitePatterns	PS00197	2Fe-2S ferredoxin-type iron-sulfur binding region signature.
323	331	InterPro	IPR006058	2Fe-2S ferredoxin, iron-sulphur binding site
3	264	SUPERFAMILY	SSF50800	PK beta-barrel domain-like
3	264	InterPro	IPR011037	Pyruvate kinase-like, insert domain superfamily
272	368	Gene3D	G3DSA:3.10.20.30	-
272	368	InterPro	IPR012675	Beta-grasp domain superfamily
4	263	PANTHER	PTHR14237	MOLYBDOPTERIN COFACTOR SULFURASE MOSC

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

0.859

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Surrounding area

Pocket 2 P2Rank #2

0.084

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Surrounding area

Pocket 3 P2Rank #3

0.057

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Surrounding area

Pocket 4 P2Rank #4

0.023

Likely same site as FPocket 13 1.8 Å 6 shared residues 100% of smaller site

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Surrounding area

Pocket 5 P2Rank #5

0.022

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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 #13

0.417

Likely same site as P2Rank 4 1.8 Å 6 shared residues 100% of smaller site

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Surrounding area

Pocket 2 FPocket #2

0.28

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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

0.749

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Surrounding area

Pocket 2 P2Rank #2

0.07

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Surrounding area

Pocket 3 P2Rank #3

0.012

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Surrounding area

Pocket 4 P2Rank #4

0.005

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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_A0A0H3GV44	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_1512	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.

61 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 11 records from similar proteins

Structural ligands 11 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

B3P PDB via homolog 282.3 Da · LogP -4.01 · TPSA 145.4 Open detail RCSB PDB

BCR PDB via homolog Detail RCSB PDB

DGD PDB via homolog Detail RCSB PDB

EFK PDB via homolog Detail RCSB PDB

FES 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
B3P RCSB PDB	6FW2	Q5VT66	282.3 Da LogP -4.01 TPSA 145.4	1 viol.	✓ Clean	`C(CNC(CO)(CO)CO)CNC(CO)(CO)CO`
BCR RCSB PDB	6L7O	P0A3C9	536.9 Da LogP 12.61 TPSA 0.0	2 viol.	✓ Clean	`CC1=C(C(CCC1)(C)C)\C=C\C(=C\C=C\C(=C\C=C\C=C(/C…`
DGD RCSB PDB	6KHI	P0A3C9	949.3 Da LogP 7.61 TPSA 231.1	4 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](CO[C@H]1[C@@H]([C…`
EFK RCSB PDB	6FW2	Q5VT66	128.9 Da LogP -0.68 TPSA 37.3	✓ Ro5	✓ Clean	`O[Mo]=O`
FES RCSB PDB	4N58	A0A067XG75	175.8 Da LogP 1.29 TPSA 0.0	✓ Ro5	✓ Clean	`S1[Fe]S[Fe]1`
LHG RCSB PDB	6KHI	P0A3C9	723.0 Da LogP 9.89 TPSA 148.8	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@…`
LMG RCSB PDB	5ZF0	P0A3C9	787.2 Da LogP 9.78 TPSA 152.0	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](CO[C@H]1[C@@H]([C…`
MOO RCSB PDB	6FW2	Q5VT66	159.9 Da LogP -2.62 TPSA 80.3	✓ Ro5	✓ Clean	`[O-][Mo](=O)(=O)[O-]`
MTE RCSB PDB	6FW2	Q5VT66	395.4 Da LogP -0.54 TPSA 171.8	1 viol.	✓ Clean	`C([C@@H]1C(=C([C@H]2[C@@H](O1)NC3=C(N2)C(=O)NC(…`
PQN RCSB PDB	5ZF0	P0A3C9	450.7 Da LogP 9.16 TPSA 34.1	1 viol.	Alert	`CC1=C(C(=O)c2ccccc2C1=O)C\C=C(/C)\CCC[C@H](C)CC…`
SQD RCSB PDB	6KHI	P0A3C9	795.1 Da LogP 8.12 TPSA 186.1	3 viol.	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](COC1[C@@H]([C@H]([C…`

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
ZINC102191119 ZINC	1.000	498.6 Da LogP 3.65 TPSA 148.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@@H](O)CO…`
ZINC4521259 ZINC	1.000	282.3 Da LogP -4.01 TPSA 145.4	1 viol.	✓ Clean	`OCC(CO)(CO)NCCCNC(CO)(CO)CO`
ZINC58649551 ZINC	1.000	498.6 Da LogP 3.65 TPSA 148.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@H](O)CO)…`
ZINC102191158 ZINC	0.795	456.5 Da LogP 3.08 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@@](=O)(O)OC[C@…`
ZINC14880758 ZINC	0.795	484.6 Da LogP 3.86 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@](=O)(O)OC[…`
ZINC14880760 ZINC	0.795	484.6 Da LogP 3.86 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@](=O)(O)OC[C…`
ZINC53683910 ZINC	0.795	484.6 Da LogP 3.86 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@@](=O)(O)OC[…`
ZINC62592202 ZINC	0.795	456.5 Da LogP 3.08 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@@](=O)(O)OC[C@…`
ZINC62592203 ZINC	0.795	456.5 Da LogP 3.08 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@@](=O)(O)OC[C…`
ZINC62592204 ZINC	0.795	484.6 Da LogP 3.86 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@@](=O)(O)OC…`
ZINC96094841 ZINC	0.795	456.5 Da LogP 3.08 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@@](=O)(O)OC[C…`
ZINC102190506 ZINC	0.729	467.5 Da LogP 4.25 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OCCN)OC(=O)CC…`
ZINC102190512 ZINC	0.729	467.5 Da LogP 4.25 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)C…`
ZINC36178999 ZINC	0.711	424.5 Da LogP 4.27 TPSA 119.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@@H](COP(=O)(O)O)OC(=O)CCCCCCC`
ZINC36179002 ZINC	0.711	424.5 Da LogP 4.27 TPSA 119.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](COP(=O)(O)O)OC(=O)CCCCCCC`
ZINC44830468 ZINC	0.711	346.5 Da LogP 4.93 TPSA 60.7	✓ Ro5	✓ Clean	`CC1=C(/C=C\C(C)=C/C=C/C(C)=C\CCC(O)(O)O)C(C)(C)…`
ZINC95908757 ZINC	0.711	346.5 Da LogP 4.93 TPSA 60.7	✓ Ro5	✓ Clean	`CC1=C(/C=C\C(C)=C/C=C\C(C)=C/CCC(O)(O)O)C(C)(C)…`
ZINC27416437 ZINC	0.708	411.4 Da LogP 2.69 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCCN)OC(=O)CCCCC`
ZINC33902364 ZINC	0.708	411.4 Da LogP 2.69 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)CCC…`
ZINC13543394 ZINC	0.694	455.4 Da LogP 2.15 TPSA 171.7	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@H](N)C(=O)…`
ZINC5820131 ZINC	0.689	368.4 Da LogP 2.71 TPSA 119.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](COP(=O)(O)O)OC(=O)CCCCC`
ZINC5820134 ZINC	0.689	368.4 Da LogP 2.71 TPSA 119.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](COP(=O)(O)O)OC(=O)CCCCC`
ZINC13544781 ZINC	0.686	482.6 Da LogP 4.22 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)OC[C@@H](CO[P@](=O)(O)OCC[N+](C)(C)C…`
ZINC13544783 ZINC	0.686	482.6 Da LogP 4.22 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCC[N+](C)(C)C)…`
ZINC13543439 ZINC	0.667	454.5 Da LogP 3.44 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](CO[P@](=O)(O)OCC[N+](C)(C)C)…`
ZINC13543441 ZINC	0.667	454.5 Da LogP 3.44 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCC[N+](C)(C)C)O…`
ZINC17284934 ZINC	0.650	234.3 Da LogP 4.10 TPSA 37.3	✓ Ro5	✓ Clean	`CC1=C(/C=C\C(C)=C/C(=O)O)C(C)(C)CCC1`
ZINC17284937 ZINC	0.650	234.3 Da LogP 4.10 TPSA 37.3	✓ Ro5	✓ Clean	`CC1=C(/C=C/C(C)=C\C(=O)O)C(C)(C)CCC1`
ZINC22061499 ZINC	0.650	220.4 Da LogP 4.01 TPSA 20.2	✓ Ro5	✓ Clean	`CC1=C(/C=C/C(C)=C/CO)C(C)(C)CCC1`
ZINC4430042 ZINC	0.650	234.3 Da LogP 4.10 TPSA 37.3	✓ Ro5	✓ Clean	`CC1=C(/C=C/C(C)=C/C(=O)O)C(C)(C)CCC1`
ZINC65748979 ZINC	0.650	214.4 Da LogP 4.65 TPSA 0.0	✓ Ro5	✓ Clean	`C#C/C=C(C)/C=C/C1=C(C)CCCC1(C)C`
ZINC8613746 ZINC	0.650	234.3 Da LogP 4.10 TPSA 37.3	✓ Ro5	✓ Clean	`CC1=C(/C=C\C(C)=C\C(=O)O)C(C)(C)CCC1`
ZINC257355159 ZINC	0.648	496.6 Da LogP -1.71 TPSA 195.6	2 viol.	✓ Clean	`CCCCCCCCCC(=O)OC[C@@H]1O[C@H](O[C@H]2O[C@H](CO)…`
ZINC257355160 ZINC	0.648	496.6 Da LogP -1.71 TPSA 195.6	2 viol.	✓ Clean	`CCCCCCCCCC(=O)OC[C@@H]1O[C@H](O[C@H]2O[C@H](CO)…`
ZINC257355161 ZINC	0.648	496.6 Da LogP -1.71 TPSA 195.6	2 viol.	✓ Clean	`CCCCCCCCCC(=O)OC[C@@H]1O[C@H](O[C@H]2O[C@H](CO)…`
ZINC257355162 ZINC	0.648	496.6 Da LogP -1.71 TPSA 195.6	2 viol.	✓ Clean	`CCCCCCCCCC(=O)OC[C@@H]1O[C@H](O[C@H]2O[C@H](CO)…`
ZINC257373326 ZINC	0.648	468.5 Da LogP -2.49 TPSA 195.6	2 viol.	✓ Clean	`CCCCCCCC(=O)OC[C@@H]1O[C@H](O[C@H]2O[C@H](CO)[C…`
ZINC257373327 ZINC	0.648	468.5 Da LogP -2.49 TPSA 195.6	2 viol.	✓ Clean	`CCCCCCCC(=O)OC[C@@H]1O[C@H](O[C@H]2O[C@H](CO)[C…`
ZINC257373328 ZINC	0.648	468.5 Da LogP -2.49 TPSA 195.6	2 viol.	✓ Clean	`CCCCCCCC(=O)OC[C@@H]1O[C@H](O[C@H]2O[C@H](CO)[C…`
ZINC257373329 ZINC	0.648	468.5 Da LogP -2.49 TPSA 195.6	2 viol.	✓ Clean	`CCCCCCCC(=O)OC[C@@H]1O[C@H](O[C@H]2O[C@H](CO)[C…`
ZINC115591405 ZINC	0.636	373.6 Da LogP 4.55 TPSA 72.7	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCCCCNC(CO)(CO)CO`
ZINC115591837 ZINC	0.636	317.5 Da LogP 2.99 TPSA 72.7	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCNC(CO)(CO)CO`
ZINC143575268 ZINC	0.636	289.5 Da LogP 2.21 TPSA 72.7	✓ Ro5	✓ Clean	`CCCCCCCCCCCCNC(CO)(CO)CO`
ZINC2322313 ZINC	0.636	233.4 Da LogP 0.65 TPSA 72.7	✓ Ro5	✓ Clean	`CCCCCCCCNC(CO)(CO)CO`
ZINC36079847 ZINC	0.636	344.5 Da LogP 4.15 TPSA 72.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@@H](CO)OC(=O)CCCCCCC`
ZINC8214428 ZINC	0.636	344.5 Da LogP 4.15 TPSA 72.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO)OC(=O)CCCCCCC`
ZINC97996983 ZINC	0.636	345.6 Da LogP 3.77 TPSA 72.7	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCCNC(CO)(CO)CO`
ZINC100503478 ZINC	0.628	260.4 Da LogP 2.41 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCCCCC(=O)OC[C@@H](O)CO`
ZINC32840884 ZINC	0.628	302.5 Da LogP 3.58 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@H](O)CO`
ZINC38153421 ZINC	0.628	246.3 Da LogP 2.02 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCCCC(=O)OC[C@@H](O)CO`

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 A0A0H3GV44