KpKP13 Protein target profile

Thioredoxin-1

Accession: KP13_13105

Gene: ANJ86649.1 trxA 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GLK1

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Length 109

Pocket druggability (P2Rank · AlphaFold DB model) 0.049

Direct ligand evidence 0 56 total records

Functional annotation 0 EC 3 GO

Target summary

Target candidate with partial support; inspect missing evidence before prioritizing.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing 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 (%): 41.86 Lower values reduce human off-target concern.
Human E-value: 9.27e-18
Gut microbiome similarity: 16.9% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 97.248 Higher values support similarity to known essential genes.
DEG E-value: 3.22e-75 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 94.17 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) 0.049

Structure A0A0H3GLK1

Pocket Pocket 1

Druggability (FPocket) 0.179

Structure A0A0H3GLK1

Pocket Pocket 5

ColabFold model

P2Rank 0.062 · Pocket 1

FPocket 0.032 · Pocket 4

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 803 / 4744 genomes with a hit

Prevalence 16.9%

Sequence

Primary amino-acid sequence viewer.

MSDKIIHLTDDSFDTDVLKADGLTLVDFWAEWCGPCKMIAPILDEIAEEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNGEVAATKVGALSKGQLKEFLDANLA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

3 GO

Subcellular localization

Localization: Cytoplasmic

Gene Ontology (GO)

GO:0015035 Catalysis of the reaction: a protein with reduced sulfide groups = a protein with oxidized disulfide bonds.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0045454 Any process that maintains the redox environment of a cell or compartment within a cell.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

19 records

Show feature table

Start	End	DB	Term	Name
25	43	ProSitePatterns	PS00194	Thioredoxin family active site.
25	43	InterPro	IPR017937	Thioredoxin, conserved site
1	108	Gene3D	G3DSA:3.40.30.10	Glutaredoxin
24	32	PRINTS	PR00421	Thioredoxin family signature
72	83	PRINTS	PR00421	Thioredoxin family signature
32	41	PRINTS	PR00421	Thioredoxin family signature
11	105	CDD	cd02947	TRX_family
1	108	FunFam	G3DSA:3.40.30.10:FF:000001	Thioredoxin
5	105	Pfam	PF00085	Thioredoxin
5	105	InterPro	IPR013766	Thioredoxin domain
2	108	PIRSF	PIRSF000077	Thioredoxin
2	108	InterPro	IPR005746	Thioredoxin
8	106	PANTHER	PTHR45663	GEO12009P1
9	107	NCBIfam	TIGR01068	thioredoxin
9	107	InterPro	IPR005746	Thioredoxin
1	109	ProSiteProfiles	PS51352	Thioredoxin domain profile.
1	109	InterPro	IPR013766	Thioredoxin domain
2	108	SUPERFAMILY	SSF52833	Thioredoxin-like
2	108	InterPro	IPR036249	Thioredoxin-like 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.

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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

0.049

Show in viewer

Surrounding area

Residue sets

UniProt: Active site:33-33 Nucleophile

UniProt: Active site:36-36 Nucleophile

UniProt: Site:27-27 Deprotonates C-terminal active site Cys

UniProt: Site:34-34 Contributes to redox potential value

UniProt: Site:35-35 Contributes to redox potential value

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_A0A0H3GLK1	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_13105	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.

56 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 6 records from similar proteins

Structural ligands 6 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

2CV PDB via homolog 379.5 Da · LogP -0.62 · TPSA 141.7 Open detail RCSB PDB

CAC PDB via homolog Detail RCSB PDB

EVU PDB via homolog Detail RCSB PDB

FVK PDB via homolog Detail RCSB PDB

GSH 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
2CV RCSB PDB	6H7N	P0AA25	379.5 Da LogP -0.62 TPSA 141.7	1 viol.	✓ Clean	`CCCCCCCCCC(=O)N(CCO)C[C@H]([C@H]([C@H]([C@H](CO…`
CAC RCSB PDB	1NW2	P80579	137.0 Da LogP -0.52 TPSA 40.1	✓ Ro5	✓ Clean	`C[As](=O)(C)[O-]`
EVU RCSB PDB	6LUR	P0AA25	281.4 Da LogP 1.75 TPSA 58.4	✓ Ro5	✓ Clean	`c1ccc(c(c1)c2ccc(cc2)CN)N3CCNC(=O)C3`
FVK RCSB PDB	6H7N	P0AA25	339.4 Da LogP -0.24 TPSA 103.3	✓ Ro5	✓ Clean	`c1cc(ccc1O)OC[C@H](CNCCNC(=O)N2CCOCC2)O`
GSH RCSB PDB	3F3R	P22217	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`
PX5 RCSB PDB	3O6T	P9WG67	243.3 Da LogP 2.18 TPSA 50.2	✓ Ro5	✓ Clean	`c1ccc2c(c1)nc(s2)C3(C=CC(=O)C=C3)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
ZINC111912619 ZINC	1.000	365.5 Da LogP -1.01 TPSA 141.7	1 viol.	✓ Clean	`CCCCCCCCC(=O)N(CCO)C[C@H](O)[C@H](O)[C@H](O)[C@…`
ZINC14880168 ZINC	1.000	365.5 Da LogP -1.01 TPSA 141.7	1 viol.	✓ Clean	`CCCCCCCCC(=O)N(CCO)C[C@H](O)[C@H](O)[C@@H](O)[C…`
ZINC1532364 ZINC	1.000	339.4 Da LogP -0.24 TPSA 103.3	✓ Ro5	✓ Clean	`O=C(NCCNC[C@@H](O)COc1ccc(O)cc1)N1CCOCC1`
ZINC1532365 ZINC	1.000	339.4 Da LogP -0.24 TPSA 103.3	✓ Ro5	✓ Clean	`O=C(NCCNC[C@H](O)COc1ccc(O)cc1)N1CCOCC1`
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`
ZINC9111 ZINC	1.000	243.3 Da LogP 2.18 TPSA 50.2	✓ Ro5	✓ Clean	`O=C1C=CC(O)(c2nc3ccccc3s2)C=C1`
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`
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`
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`
ZINC3778474 ZINC	0.727	349.4 Da LogP -1.34 TPSA 147.8	✓ Ro5	✓ Clean	`CC(C)OC(=O)CNC(=O)[C@H](CS)NC(=O)CC[C@H](N)C(=O…`
ZINC3778476 ZINC	0.727	335.4 Da LogP -1.73 TPSA 147.8	✓ Ro5	✓ Clean	`CCOC(=O)CNC(=O)[C@H](CS)NC(=O)CC[C@H](N)C(=O)O`
ZINC5497203 ZINC	0.727	335.4 Da LogP -1.73 TPSA 147.8	✓ Ro5	✓ Clean	`CCOC(=O)CNC(=O)[C@@H](CS)NC(=O)CC[C@H](N)C(=O)O`
ZINC5497237 ZINC	0.727	335.4 Da LogP -1.73 TPSA 147.8	✓ Ro5	✓ Clean	`CCOC(=O)CNC(=O)[C@@H](CS)NC(=O)CC[C@@H](N)C(=O)O`
ZINC5497239 ZINC	0.727	335.4 Da LogP -1.73 TPSA 147.8	✓ Ro5	✓ Clean	`CCOC(=O)CNC(=O)[C@H](CS)NC(=O)CC[C@@H](N)C(=O)O`
ZINC1532230 ZINC	0.714	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	0.714	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	0.714	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	0.714	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`
ZINC1532902 ZINC	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@@](O)(CC(=O)O)C(=O)O`
ZINC2018106 ZINC	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@](O)(CC(=O)O)C(=O)O`
ZINC1616624 ZINC	0.698	355.3 Da LogP -3.25 TPSA 213.2	1 viol.	✓ Clean	`N[C@@H](CCC(=O)N[C@@H](CS(=O)(=O)O)C(=O)NCC(=O)…`
ZINC1616625 ZINC	0.698	355.3 Da LogP -3.25 TPSA 213.2	1 viol.	✓ Clean	`N[C@@H](CCC(=O)N[C@H](CS(=O)(=O)O)C(=O)NCC(=O)O…`
ZINC1616626 ZINC	0.698	355.3 Da LogP -3.25 TPSA 213.2	1 viol.	✓ Clean	`N[C@H](CCC(=O)N[C@@H](CS(=O)(=O)O)C(=O)NCC(=O)O…`
ZINC1616627 ZINC	0.698	355.3 Da LogP -3.25 TPSA 213.2	1 viol.	✓ Clean	`N[C@H](CCC(=O)N[C@H](CS(=O)(=O)O)C(=O)NCC(=O)O)…`
ZINC100056640 ZINC	0.675	335.4 Da LogP -0.37 TPSA 121.5	✓ Ro5	✓ Clean	`CCCCCCCCC(=O)N(C)C[C@H](O)[C@H](O)[C@@H](O)[C@@…`
ZINC100056652 ZINC	0.675	349.5 Da LogP 0.02 TPSA 121.5	✓ Ro5	✓ Clean	`CCCCCCCCCC(=O)N(C)C[C@H](O)[C@H](O)[C@@H](O)[C@…`
ZINC104829077 ZINC	0.675	321.4 Da LogP -0.76 TPSA 121.5	✓ Ro5	✓ Clean	`CCCCCCCC(=O)N(C)C[C@H](O)[C@H](O)[C@@H](O)[C@H]…`
ZINC12496578 ZINC	0.675	275.3 Da LogP -2.12 TPSA 158.8	✓ Ro5	✓ Clean	`C[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC169497114 ZINC	0.675	321.4 Da LogP -0.76 TPSA 121.5	✓ Ro5	✓ Clean	`CCCCCCCC(=O)N(C)C[C@H](O)[C@H](O)[C@@H](O)[C@@H…`
ZINC238808944 ZINC	0.675	335.4 Da LogP -0.37 TPSA 121.5	✓ Ro5	✓ Clean	`CCCCCCCCC(=O)N(C)C[C@H](O)[C@H](O)[C@H](O)[C@@H…`
ZINC238808945 ZINC	0.675	335.4 Da LogP -0.37 TPSA 121.5	✓ Ro5	✓ Clean	`CCCCCCCCC(=O)N(C)C[C@H](O)[C@H](O)[C@@H](O)[C@H…`
ZINC238809466 ZINC	0.675	349.5 Da LogP 0.02 TPSA 121.5	✓ Ro5	✓ Clean	`CCCCCCCCCC(=O)N(C)C[C@H](O)[C@H](O)[C@@H](O)[C@…`
ZINC238809467 ZINC	0.675	349.5 Da LogP 0.02 TPSA 121.5	✓ Ro5	✓ Clean	`CCCCCCCCCC(=O)N(C)C[C@H](O)[C@H](O)[C@H](O)[C@@…`
ZINC248290074 ZINC	0.675	321.4 Da LogP -0.76 TPSA 121.5	✓ Ro5	✓ Clean	`CCCCCCCC(=O)N(C)C[C@H](O)[C@H](O)[C@H](O)[C@@H]…`
ZINC38377620 ZINC	0.675	321.4 Da LogP -0.76 TPSA 121.5	✓ Ro5	✓ Clean	`CCCCCCCC(=O)N(C)C[C@H](O)[C@H](O)[C@H](O)[C@H](…`
ZINC71788547 ZINC	0.675	349.5 Da LogP 0.02 TPSA 121.5	✓ Ro5	✓ Clean	`CCCCCCCCCC(=O)N(C)C[C@H](O)[C@H](O)[C@H](O)[C@H…`
ZINC71788549 ZINC	0.675	349.5 Da LogP 0.02 TPSA 121.5	✓ Ro5	✓ Clean	`CCCCCCCCCC(=O)N(C)C[C@H](O)[C@@H](O)[C@H](O)[C@…`
ZINC71788557 ZINC	0.675	321.4 Da LogP -0.76 TPSA 121.5	✓ Ro5	✓ Clean	`CCCCCCCC(=O)N(C)C[C@H](O)[C@@H](O)[C@H](O)[C@H]…`
ZINC71788568 ZINC	0.675	335.4 Da LogP -0.37 TPSA 121.5	✓ Ro5	✓ Clean	`CCCCCCCCC(=O)N(C)C[C@H](O)[C@H](O)[C@H](O)[C@H]…`
ZINC71788570 ZINC	0.675	335.4 Da LogP -0.37 TPSA 121.5	✓ Ro5	✓ Clean	`CCCCCCCCC(=O)N(C)C[C@H](O)[C@@H](O)[C@H](O)[C@H…`
ZINC3872733 ZINC	0.667	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	0.667	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`

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 A0A0H3GLK1

Thioredoxin-1

Target candidate with partial support; inspect missing evidence before prioritizing.

Main supporting evidence

Risks to review

Evidence gaps

Prioritization evidence

Off-target risk

Essentiality

Structure confidence

Binding-site evidence

Sequence

Functional annotations

Subcellular localization

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · P2Rank

Binding pockets · P2Rank

Structural evidence

Ligand evidence

Cross-references

Sequence