Genome KpKP13

Protein target profile

Glutaredoxin-1

Accession: KP13_04260

Gene: AHE45490.1 grxA 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GUS3

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Length 87

Pocket druggability (P2Rank · AlphaFold DB model) 0.018

Direct ligand evidence 0 53 total records

Functional annotation 0 EC 7 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 (%): 32.099 Lower values reduce human off-target concern.
Human E-value: 1.21e-07
Gut microbiome similarity: 2.9% 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: 86.79 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) 0.018

Structure A0A0H3GUS3

Pocket Pocket 1

Druggability (FPocket) 0.391

Structure A0A0H3GUS3

Pocket Pocket 3

ColabFold model

FPocket 0.323 · Pocket 3

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 138 / 4744 genomes with a hit

Prevalence 2.9%

Cross-references

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

Sequence

UniProt A0A0H3GUS3

Sequence

Primary amino-acid sequence viewer.

MFTVIFGRPGCPYCVRAKELAEKLTNERDDFNYRYVDIHAEGISKADLEKTVGKPVETVPQIFVDQKHIGGCTDFEAWAKENLGLFA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

7 GO

Subcellular localization

Localization: Unknown

Gene Ontology (GO)

GO:0009055 A molecular function representing the directed movement of electrons from one molecular entity to another, typically mediated by electron carriers or acceptors, resulting in the transfer of energy and/or the reduction-oxidation (redox) transformation of chemical species. This activity is fundamental to various biological processes, including cellular respiration and photosynthesis, as well as numerous enzymatic reactions involved in metabolic pathways.
GO:0015035 Catalysis of the reaction: a protein with reduced sulfide groups = a protein with oxidized disulfide bonds.
GO:0045454 Any process that maintains the redox environment of a cell or compartment within a cell.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0015038 Catalysis of the reaction: 2 glutathione + electron acceptor = glutathione disulfide + electron donor.
GO:0034599 Any process that results in a change in state or activity of a cell (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.
GO:0009263 The chemical reactions and pathways resulting in the formation of a deoxyribonucleotide, a compound consisting of deoxyribonucleoside (a base linked to a deoxyribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

18 records

Show feature table

Start	End	DB	Term	Name
4	80	CDD	cd02066	GRX_family
1	87	ProSiteProfiles	PS51354	Glutaredoxin domain profile.
4	80	PANTHER	PTHR45694	GLUTAREDOXIN 2
4	69	Pfam	PF00462	Glutaredoxin
4	69	InterPro	IPR002109	Glutaredoxin
5	20	ProSitePatterns	PS00195	Glutaredoxin active site.
5	20	InterPro	IPR011767	Glutaredoxin active site
3	84	Gene3D	G3DSA:3.40.30.10	Glutaredoxin
2	86	NCBIfam	TIGR02183	glutaredoxin, GrxA family
2	86	InterPro	IPR011902	Glutaredoxin, GrxA
4	82	SUPERFAMILY	SSF52833	Thioredoxin-like
4	82	InterPro	IPR036249	Thioredoxin-like superfamily
3	21	PRINTS	PR00160	Glutaredoxin signature
3	21	InterPro	IPR014025	Glutaredoxin subgroup
66	79	PRINTS	PR00160	Glutaredoxin signature
66	79	InterPro	IPR014025	Glutaredoxin subgroup
52	65	PRINTS	PR00160	Glutaredoxin signature
52	65	InterPro	IPR014025	Glutaredoxin subgroup

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

0.018

Likely same site as FPocket 3 3.6 Å 6 shared residues 86% 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 #3

0.391

Likely same site as P2Rank 1 3.6 Å 6 shared residues 86% of smaller site

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_A0A0H3GUS3	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_04260	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.

53 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 3 records from similar proteins

Structural ligands 3 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

CAC PDB via homolog 137.0 Da · LogP -0.52 · TPSA 40.1 Open detail RCSB PDB

COM PDB via homolog Detail RCSB PDB

GSH PDB via homolog Detail RCSB PDB

ZINC3830891 ZINC proposed compound · Tanimoto 1.000 Detail ZINC

ZINC3830892 ZINC proposed compound · Tanimoto 1.000 Detail ZINC

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
CAC RCSB PDB	3MSZ	Q5NHD0	137.0 Da LogP -0.52 TPSA 40.1	✓ Ro5	✓ Clean	`C[As](=O)(C)[O-]`
COM RCSB PDB	4RQR	P35754	142.2 Da LogP -0.20 TPSA 54.4	✓ Ro5	✓ Clean	`C(CS(=O)(=O)O)S`
GSH RCSB PDB	3GRX	P0AC62	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`

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
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`
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`
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)…`
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`
ZINC13522300 ZINC	0.667	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	0.667	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	0.667	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	0.667	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	0.667	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…`
ZINC3872732 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`
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`
ZINC3872734 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`
ZINC4544083 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`
ZINC4544084 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`
ZINC4544085 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`
ZINC13451235 ZINC	0.652	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	0.652	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	0.652	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	0.652	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	0.652	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	0.652	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	0.652	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	0.652	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(…`
ZINC3920510 ZINC	0.652	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	0.652	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…`
ZINC13507523 ZINC	0.643	303.3 Da LogP -1.48 TPSA 158.8	✓ Ro5	✓ Clean	`CC(C)[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC4899752 ZINC	0.641	235.3 Da LogP -2.44 TPSA 121.5	✓ Ro5	✓ Clean	`NCC(=O)N[C@@H](CS)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.

Glutaredoxin-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

Cross-references

Sequence

Sequence

Functional annotations

Subcellular localization

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · P2Rank

Binding pockets · FPocket

Binding pockets · P2Rank

Binding pockets · FPocket

Structural evidence

Ligand evidence