Protein target profile

VK055_2450

dihydrolipoyl dehydrogenase

Genome: KpATCC43816 Gene: AIK81047.1 lpdA2 3D evidence: AlphaFold DB model + ColabFold model Metabolism 6 reactions UniProt A0A0H3GJD9

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Length 474

Pocket druggability 0.981

Metabolic reactions 6

Chokepoint Yes

Direct ligand evidence 0 71 total records

Functional annotation 1 EC 7 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

Metabolic bottleneck Catalyzes a reaction that is the only producer or consumer of a metabolite in the imported metabolic model. Central metabolic position More central than 95.1% of genes in this genome. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Second pocket predictor agrees P2Rank predicted binding-site probability 0.95. 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 (%): 52.778 Lower values reduce human off-target concern.
Human E-value: 7.09e-16
Gut microbiome similarity: 3.6% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 98.312 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 97.1 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

The selected pocket score is the FPocket value used for ranking after applying the curated structure priority. It estimates small-molecule pocket quality; it is not experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

FPocket 0.981

Structure A0A0H3GJD9

Pocket Pocket 33

P2Rank 0.953

Structure A0A0H3GJD9

Pocket Pocket 1

ColabFold model

FPocket 0.923 · Pocket 28

P2Rank 0.982 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 172 / 4744 genomes with a hit

Prevalence 3.6%

Cross-references

External database identifiers for this protein, its structures, ligands, and metabolic reactions.

Metabolic context

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

Explore metabolic network

Attractive metabolic target: catalyzes a producing & consuming chokepoint reaction, more central than 95.1% of genes in this genome.

Relative network centrality 95.1% more central than 95.1% of genes in this genome

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MSTEIKTQVVVLGAGPAGYSAAFRCADLGLETVIVERYSTLGGVCLNVGCIPSKALLHVAKVIEEAKALAEHGIVFGEPKTDIDKIRTWKEKVITQLTGGLAGMAKGRKVKVVNGLGKFTGANTLEVEGENGKTVINFDNAIIAAGSRPIQLPFIPHEDPRVWDSTDALELKSVPKRMLVMGGGIIGLEMGTVYHALGSEIDVVEMFDQVIPAADKDVVKVFTKRISKKFNLMLETKVTAVEAKEDGIYVSMEGKKAPAEAQRYDAVLVAIGRVPNGKNLDAGKAGVEVDDRGFIRVDKQMRTNVPHIFAIGDIVGQPMLAHKGVHEGHVAAEVISGLKHYFDPKVIPSIAYTEPEVAWVGLTEKEAKEKGISYETATFPWAASGRAIASDCADGMTKLIFDKETHRVIGGAIVGTNGGELLGEIGLAIEMGCDAEDIALTIHAHPTLHESVGLAAEVFEGSITDLPNAKAKKK

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Enzyme Commission (EC)

1.8.1.4

Gene Ontology (GO)

GO:0004148 Catalysis of the reaction: N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD+ = N(6)-[(R)-lipoyl]-L-lysyl-[protein] + NADH + H+.
GO:0016668 Catalysis of an oxidation-reduction (redox) reaction in which a sulfur-containing group acts as a hydrogen or electron donor and reduces NAD or NADP.
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:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0006103 The chemical reactions and pathways involving oxoglutarate, the dianion of 2-oxoglutaric acid. It is a key constituent of the TCA cycle and a key intermediate in amino-acid metabolism.
GO:0006979 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

38 records

Show feature table

Start	End	DB	Term	Name
347	455	Pfam	PF02852	Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain
347	455	InterPro	IPR004099	Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain
4	458	PANTHER	PTHR22912	DISULFIDE OXIDOREDUCTASE
346	467	Gene3D	G3DSA:3.30.390.30	-
346	467	InterPro	IPR016156	FAD/NAD-linked reductase, dimerisation domain superfamily
7	460	NCBIfam	TIGR01350	dihydrolipoyl dehydrogenase
7	460	InterPro	IPR006258	Dihydrolipoamide dehydrogenase
343	466	SUPERFAMILY	SSF55424	FAD/NAD-linked reductases, dimerisation (C-terminal) domain
343	466	InterPro	IPR016156	FAD/NAD-linked reductase, dimerisation domain superfamily
1	469	PIRSF	PIRSF000350	Hg-II_reductase_MerA
1	469	InterPro	IPR001100	Pyridine nucleotide-disulphide oxidoreductase, class I
7	154	FunFam	G3DSA:3.50.50.60:FF:000001	Dihydrolipoyl dehydrogenase, mitochondrial
346	466	FunFam	G3DSA:3.30.390.30:FF:000001	Dihydrolipoyl dehydrogenase
150	271	Gene3D	G3DSA:3.50.50.60	-
150	271	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
408	423	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
141	150	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
430	450	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
177	202	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
343	364	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
41	56	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
265	279	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
308	315	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
8	30	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
2	337	SUPERFAMILY	SSF51905	FAD/NAD(P)-binding domain
2	337	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
9	333	Gene3D	G3DSA:3.50.50.60	-
9	333	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
264	280	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
293	315	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
9	28	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
138	156	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
177	195	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
155	271	FunFam	G3DSA:3.50.50.60:FF:000014	Dihydrolipoyl dehydrogenase
8	328	Pfam	PF07992	Pyridine nucleotide-disulphide oxidoreductase
8	328	InterPro	IPR023753	FAD/NAD(P)-binding domain
42	52	ProSitePatterns	PS00076	Pyridine nucleotide-disulphide oxidoreductases class-I active site.
42	52	InterPro	IPR012999	Pyridine nucleotide-disulphide oxidoreductase, class I, active site

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 · FPocket

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

Site 1 FPocket #33

0.981

Likely same site as P2Rank 1 4.2 Å 42 shared residues 98% of smaller site

Unusual size

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Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.953

Likely same site as FPocket 33 4.2 Å 42 shared residues 98% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.333

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Surrounding area

Site 3 P2Rank #3

0.111

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Surrounding area

Site 4 P2Rank #4

0.051

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Surrounding area

Site 5 P2Rank #5

0.046

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Surrounding area

Residue sets

UniProt: Active site:445-445 Proton acceptor

UniProt: Binding site:117-117

UniProt: Binding site:182-189

UniProt: Binding site:205-205

UniProt: Binding site:272-272

UniProt: Binding site:313-313

UniProt: Binding site:319-322

UniProt: Binding site:54-54

Binding pockets · FPocket

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

Site 1 FPocket #28

0.923

Likely same site as P2Rank 1 3.2 Å 60 shared residues 92% of smaller site

Unusual size

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Surrounding area

Site 2 FPocket #27

0.291

Likely same site as P2Rank 4 7.3 Å 2 shared residues 33% of smaller site

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Surrounding area

Site 3 FPocket #22

0.241

Likely same site as P2Rank 3 1.7 Å 11 shared residues 92% of smaller site

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Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.982

Likely same site as FPocket 28 3.2 Å 60 shared residues 92% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.067

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Surrounding area

Site 3 P2Rank #3

0.059

Likely same site as FPocket 22 1.7 Å 11 shared residues 92% of smaller site

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Surrounding area

Site 4 P2Rank #4

0.02

Likely same site as FPocket 27 7.3 Å 2 shared residues 33% of smaller site

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Surrounding area

Site 5 P2Rank #5

0.012

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Surrounding area

Residue sets

UniProt: Active site:445-445 Proton acceptor

UniProt: Binding site:117-117

UniProt: Binding site:182-189

UniProt: Binding site:205-205

UniProt: Binding site:272-272

UniProt: Binding site:313-313

UniProt: Binding site:319-322

UniProt: Binding site:54-54

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_A0A0H3GJD9	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_2450	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.

71 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 21 records from similar proteins

Structural ligands 14 0 loaded crystals

Measured bioactivity 7 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

3II PDB via homolog 625.6 Da · LogP 4.65 · TPSA 91.4 Open detail RCSB PDB

ACM PDB via homolog Detail RCSB PDB

AUP PDB via homolog Detail RCSB PDB

BTB PDB via homolog Detail RCSB PDB

ELI 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
3II RCSB PDB	3II4	P9WHH9	625.6 Da LogP 4.65 TPSA 91.4	1 viol.	✓ Clean	`COc1ccc(c(c1)OC)C(=O)N2CCC3(CC2)C(=O)N(CN3c4ccc…`
ACM RCSB PDB	1GRF	P00390	59.1 Da LogP -0.51 TPSA 43.1	✓ Ro5	✓ Clean	`CC(=O)N`
AUP RCSB PDB	2AAQ	P00390	368.4 Da LogP 6.67 TPSA 25.8	1 viol.	✓ Clean	`c1ccc(cc1)p2c(c3c(c2c4ccccn4)CCCC3)c5ccccn5`
BTB RCSB PDB	5NHG	P09622-2	209.2 Da LogP -3.01 TPSA 104.4	✓ Ro5	✓ Clean	`C(CO)N(CCO)C(CO)(CO)CO`
ELI RCSB PDB	2GH5	P00390	286.3 Da LogP 3.42 TPSA 71.4	✓ Ro5	Alert	`CC1=C(C(=O)c2ccccc2C1=O)CCCCCC(=O)O`
GCG RCSB PDB	4GRT	P00390	723.9 Da LogP -4.58 TPSA 313.3	3 viol.	✓ Clean	`C(CCNC(=O)CNC(=O)[C@H](CS)NC(=O)CC[C@@H](C(=O)O…`
GDS RCSB PDB	2GRT	P00390	612.6 Da LogP -3.88 TPSA 317.6	3 viol.	✓ Clean	`C(CC(=O)N[C@@H](CSSC[C@@H](C(=O)NCC(=O)O)NC(=O)…`
GSH RCSB PDB	1DNC	P00390	307.3 Da LogP -2.21 TPSA 158.8	1 viol.	✓ Clean	`C(CC(=O)N[C@@H](CS)C(=O)NCC(=O)O)[C@@H](C(=O)O)N`
HXP RCSB PDB	1XAN	P00390	286.3 Da LogP 3.20 TPSA 87.0	✓ Ro5	✓ Clean	`c1cc2c(cc1O)Oc3cc(ccc3C2CCC(=O)O)O`
MLT RCSB PDB	6CMZ	B4EEF2	134.1 Da LogP -1.09 TPSA 94.8	✓ Ro5	✓ Clean	`C([C@H](C(=O)O)O)C(=O)O`
NHE RCSB PDB	3RNM	P09622-2	207.3 Da LogP 0.80 TPSA 66.4	✓ Ro5	✓ Clean	`C1CCC(CC1)NCCS(=O)(=O)O`
RGS RCSB PDB	4GR1	P00390	612.6 Da LogP -3.88 TPSA 317.6	3 viol.	✓ Clean	`C(CNC(=O)[C@@H](CSSC[C@H](C(=O)NCC[C@@H](C(=O)O…`
TS2 RCSB PDB	3GRT	P00390	721.9 Da LogP -4.04 TPSA 313.3	3 viol.	✓ Clean	`C1CCNC(=O)CNC(=O)[C@H](CSSC[C@@H](C(=O)NCC(=O)N…`
TS4 RCSB PDB	5GRT	P00390	867.1 Da LogP -4.38 TPSA 377.3	3 viol.	✓ Clean	`C(CCNCCCNC(=O)CNC(=O)[C@H](CSSC[C@@H](C(=O)NCC(…`

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).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
CHEMBL1451931 ChEMBL	P9WHH9	7.00 ~100.0 nM	263.3 Da LogP 2.58 TPSA 46.2	✓ Ro5	Alert	`O=C1C=C(NCc2ccccc2)c2ccccc2C1=O`
CHEMBL3949128 ChEMBL	P9WHH9	6.16 ~691.8 nM	463.7 Da LogP 2.35 TPSA 114.6	✓ Ro5	✓ Clean	`COc1ccc(NC(=O)CN(C)S(=O)(=O)c2cc(Br)cnc2N)cc1Cl`
CHEMBL135536 ChEMBL	P00390	6.12 ~758.6 nM	302.3 Da LogP 3.12 TPSA 91.7	✓ Ro5	Alert	`CC1=C(CCCCCC(=O)O)C(=O)c2c(O)cccc2C1=O`
CHEMBL3935059 ChEMBL	P9WHH9	6.08 ~831.8 nM	441.4 Da LogP 2.81 TPSA 105.4	✓ Ro5	✓ Clean	`CC(C)c1ccc(NC(=O)CN(C)S(=O)(=O)c2cc(Br)cnc2N)cc1`
CHEMBL3983097 ChEMBL	P9WHH9	6.08 ~831.8 nM	459.3 Da LogP 1.70 TPSA 123.9	✓ Ro5	✓ Clean	`COc1ccc(NC(=O)CN(C)S(=O)(=O)c2cc(Br)cnc2N)cc1OC`
M52 ChEMBL	P9WHH9	6.02 ~955.0 nM	429.3 Da LogP 1.69 TPSA 114.6	✓ Ro5	✓ Clean	`C[N@@](CC(=O)Nc1ccc(cc1)OC)S(=O)(=O)c2cc(cnc2N)…`
CHEMBL135504 ChEMBL	P00390	6.00 ~1.0 µM	288.3 Da LogP 2.73 TPSA 91.7	✓ Ro5	Alert	`CC1=C(CCCCC(=O)O)C(=O)c2c(O)cccc2C1=O`

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
ZINC1615342 ZINC	1.000	209.2 Da LogP -3.01 TPSA 104.4	✓ Ro5	✓ Clean	`OCCN(CCO)C(CO)(CO)CO`
ZINC1710230 ZINC	1.000	207.3 Da LogP 0.80 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCNC1CCCCC1`
ZINC3830891 ZINC	1.000	307.3 Da LogP -2.21 TPSA 158.8	1 viol.	✓ Clean	`N[C@@H](CCC(=O)N[C@@H](CS)C(=O)NCC(=O)O)C(=O)O`
ZINC3830892 ZINC	1.000	307.3 Da LogP -2.21 TPSA 158.8	1 viol.	✓ Clean	`N[C@@H](CCC(=O)N[C@H](CS)C(=O)NCC(=O)O)C(=O)O`
ZINC3830893 ZINC	1.000	307.3 Da LogP -2.21 TPSA 158.8	1 viol.	✓ Clean	`N[C@H](CCC(=O)N[C@@H](CS)C(=O)NCC(=O)O)C(=O)O`
ZINC3830894 ZINC	1.000	307.3 Da LogP -2.21 TPSA 158.8	1 viol.	✓ Clean	`N[C@H](CCC(=O)N[C@H](CS)C(=O)NCC(=O)O)C(=O)O`
ZINC1532230 ZINC	0.825	321.4 Da LogP -1.77 TPSA 158.8	✓ Ro5	✓ Clean	`CSC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC4556979 ZINC	0.825	321.4 Da LogP -1.77 TPSA 158.8	✓ Ro5	✓ Clean	`CSC[C@@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC4556980 ZINC	0.825	321.4 Da LogP -1.77 TPSA 158.8	✓ Ro5	✓ Clean	`CSC[C@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC4556981 ZINC	0.825	321.4 Da LogP -1.77 TPSA 158.8	✓ Ro5	✓ Clean	`CSC[C@@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC5828410 ZINC	0.821	306.3 Da LogP -2.81 TPSA 164.6	1 viol.	✓ Clean	`NC(=O)CNC(=O)[C@H](CS)NC(=O)CC[C@H](N)C(=O)O`
ZINC2004372 ZINC	0.786	221.3 Da LogP 1.19 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCCNC1CCCCC1`
ZINC38364153 ZINC	0.786	235.3 Da LogP 1.58 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCCCNC1CCCCC1`
ZINC4262829 ZINC	0.781	263.3 Da LogP 2.74 TPSA 46.2	✓ Ro5	Alert	`O=C1C=C(NCc2ccccc2)C(=O)c2ccccc21`
ZINC13549503 ZINC	0.780	321.4 Da LogP -2.12 TPSA 147.8	✓ Ro5	✓ Clean	`COC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(=O)O`
ZINC4096455 ZINC	0.775	321.4 Da LogP -1.82 TPSA 158.8	1 viol.	✓ Clean	`N[C@@H](CCC(=O)N[C@@H](CS)C(=O)NCCC(=O)O)C(=O)O`
ZINC13522300 ZINC	0.767	349.4 Da LogP -1.86 TPSA 175.9	✓ Ro5	✓ Clean	`CC(=O)SC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NCC(=…`
ZINC31350707 ZINC	0.767	349.4 Da LogP -1.86 TPSA 175.9	✓ Ro5	✓ Clean	`CC(=O)SC[C@@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)NCC…`
ZINC31350710 ZINC	0.767	349.4 Da LogP -1.86 TPSA 175.9	✓ Ro5	✓ Clean	`CC(=O)SC[C@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)NCC(…`
ZINC31350713 ZINC	0.767	349.4 Da LogP -1.86 TPSA 175.9	✓ Ro5	✓ Clean	`CC(=O)SC[C@@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NCC(…`
ZINC3872731 ZINC	0.767	336.3 Da LogP -1.72 TPSA 188.2	✓ Ro5	✓ Clean	`N[C@@H](CCC(=O)N[C@@H](CSN=O)C(=O)NCC(=O)O)C(=O…`
ZINC3872732 ZINC	0.767	336.3 Da LogP -1.72 TPSA 188.2	✓ Ro5	✓ Clean	`N[C@@H](CCC(=O)N[C@H](CSN=O)C(=O)NCC(=O)O)C(=O)O`
ZINC3872733 ZINC	0.767	336.3 Da LogP -1.72 TPSA 188.2	✓ Ro5	✓ Clean	`N[C@H](CCC(=O)N[C@@H](CSN=O)C(=O)NCC(=O)O)C(=O)O`
ZINC3872734 ZINC	0.767	336.3 Da LogP -1.72 TPSA 188.2	✓ Ro5	✓ Clean	`N[C@H](CCC(=O)N[C@H](CSN=O)C(=O)NCC(=O)O)C(=O)O`
ZINC4544082 ZINC	0.767	335.4 Da LogP -1.38 TPSA 158.8	✓ Ro5	✓ Clean	`CCSC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC4544083 ZINC	0.767	335.4 Da LogP -1.38 TPSA 158.8	✓ Ro5	✓ Clean	`CCSC[C@@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC4544084 ZINC	0.767	335.4 Da LogP -1.38 TPSA 158.8	✓ Ro5	✓ Clean	`CCSC[C@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC4544085 ZINC	0.767	335.4 Da LogP -1.38 TPSA 158.8	✓ Ro5	✓ Clean	`CCSC[C@@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC13451235 ZINC	0.750	423.4 Da LogP -2.47 TPSA 233.4	1 viol.	✓ Clean	`N[C@@H](CCC(=O)N[C@@H](CS[C@H](CC(=O)O)C(=O)O)C…`
ZINC145953214 ZINC	0.750	365.4 Da LogP -2.02 TPSA 179.0	1 viol.	✓ Clean	`C[C@H](O)CSC[C@@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O…`
ZINC145953600 ZINC	0.750	365.4 Da LogP -2.02 TPSA 179.0	1 viol.	✓ Clean	`C[C@H](O)CSC[C@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)…`
ZINC14966489 ZINC	0.750	423.4 Da LogP -2.47 TPSA 233.4	1 viol.	✓ Clean	`N[C@H](CCC(=O)N[C@@H](CS[C@@H](CC(=O)O)C(=O)O)C…`
ZINC14966492 ZINC	0.750	423.4 Da LogP -2.47 TPSA 233.4	1 viol.	✓ Clean	`N[C@H](CCC(=O)N[C@H](CS[C@@H](CC(=O)O)C(=O)O)C(…`
ZINC201224060 ZINC	0.750	365.4 Da LogP -2.02 TPSA 179.0	1 viol.	✓ Clean	`C[C@H](O)CSC[C@@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)…`
ZINC253638410 ZINC	0.750	423.4 Da LogP -2.47 TPSA 233.4	1 viol.	✓ Clean	`N[C@H](CCC(=O)N[C@H](CS[C@H](CC(=O)O)C(=O)O)C(=…`
ZINC253638411 ZINC	0.750	423.4 Da LogP -2.47 TPSA 233.4	1 viol.	✓ Clean	`N[C@H](CCC(=O)N[C@@H](CS[C@H](CC(=O)O)C(=O)O)C(…`
ZINC2554974 ZINC	0.750	289.3 Da LogP -1.73 TPSA 158.8	✓ Ro5	✓ Clean	`CC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC3870040 ZINC	0.750	250.3 Da LogP -1.32 TPSA 129.7	✓ Ro5	✓ Clean	`N[C@@H](CCC(=O)N[C@@H](CS)C(=O)O)C(=O)O`
ZINC3870041 ZINC	0.750	250.3 Da LogP -1.32 TPSA 129.7	✓ Ro5	✓ Clean	`N[C@@H](CCC(=O)N[C@H](CS)C(=O)O)C(=O)O`
ZINC3870042 ZINC	0.750	250.3 Da LogP -1.32 TPSA 129.7	✓ Ro5	✓ Clean	`N[C@H](CCC(=O)N[C@@H](CS)C(=O)O)C(=O)O`
ZINC3870043 ZINC	0.750	250.3 Da LogP -1.32 TPSA 129.7	✓ Ro5	✓ Clean	`N[C@H](CCC(=O)N[C@H](CS)C(=O)O)C(=O)O`
ZINC3920510 ZINC	0.750	423.4 Da LogP -2.47 TPSA 233.4	1 viol.	✓ Clean	`N[C@@H](CCC(=O)N[C@@H](CS[C@@H](CC(=O)O)C(=O)O)…`
ZINC77300920 ZINC	0.750	365.4 Da LogP -2.02 TPSA 179.0	1 viol.	✓ Clean	`C[C@H](O)CSC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)N…`
ZINC4556756 ZINC	0.733	377.4 Da LogP -2.29 TPSA 193.0	✓ Ro5	✓ Clean	`CC(=O)C(=O)SC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)…`
ZINC4556757 ZINC	0.733	377.4 Da LogP -2.29 TPSA 193.0	✓ Ro5	✓ Clean	`CC(=O)C(=O)SC[C@@H](NC(=O)CC[C@H](N)C(=O)O)C(=O…`
ZINC4556758 ZINC	0.733	377.4 Da LogP -2.29 TPSA 193.0	✓ Ro5	✓ Clean	`CC(=O)C(=O)SC[C@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O…`
ZINC4556759 ZINC	0.733	377.4 Da LogP -2.29 TPSA 193.0	✓ Ro5	✓ Clean	`CC(=O)C(=O)SC[C@@H](NC(=O)CC[C@@H](N)C(=O)O)C(=…`
ZINC504173140 ZINC	0.733	365.4 Da LogP -2.02 TPSA 179.0	1 viol.	✓ Clean	`C[C@H](CO)SC[C@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)…`
ZINC5883749 ZINC	0.733	364.4 Da LogP -2.06 TPSA 187.9	1 viol.	✓ Clean	`CNC(=O)SC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NCC(…`
ZINC5883754 ZINC	0.733	364.4 Da LogP -2.06 TPSA 187.9	1 viol.	✓ Clean	`CNC(=O)SC[C@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)NCC…`

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.

VK055_2450

Strong target candidate with converging metabolic, structural and chemical evidence.

Main supporting evidence

Risks to review

Evidence coverage

Prioritization evidence

Off-target risk

Essentiality

Localization

Structure confidence

Binding-site evidence

Cross-references

Sequence

Chemistry

Pathways

Metabolic context

Sequence

Functional annotations

Enzyme Commission (EC)

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · FPocket

Binding pockets · P2Rank

Binding pockets · FPocket

Binding pockets · P2Rank

Structural evidence

Ligand evidence