Protein profile

KP13_00211

Glutaredoxin-3

Genome: KpKP13

Gene: grxC AHE42124.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GYR4
Amino acids 83
Annotations 5
Features 20
PDB binders 3
Druggability 0.195

Overview

Basic information about this protein and its source genome.

Accession
KP13_00211
Gene
grxC AHE42124.1
Status
annotated
Amino acids
83
Structure source
AlphaFold + ColabFold

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
34.118
Human E-value
3.47e-10
Gut microbiome off-target
hit
Essential (DEG)
Y
DEG identity (%)
50.0
DEG E-value
2.22e-25
Localization
Unknown
ColabFold pLDDT
93.51

Selected Druggability evidence

AlphaFold / UniProt model

Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.

FPocket 0.195
Structure A0A0H3GYR4
Pocket Pocket 2
P2Rank
Structure A0A0H3GYR4
Pocket No pockets
ColabFold model
FPocket 0.154 · Pocket 2
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 131 / 4744 genomes with a hit
Normalized 0.028

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

5 GO

Gene Ontology (GO)

5
  • 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 Features

Domain/signature hits from InterPro and related databases.

20 records
Show feature table
Start End DB Term Name
1 83 Gene3D G3DSA:3.40.30.10 Glutaredoxin
6 22 ProSitePatterns PS00195 Glutaredoxin active site.
6 22 InterPro IPR011767 Glutaredoxin active site
4 63 Pfam PF00462 Glutaredoxin
4 63 InterPro IPR002109 Glutaredoxin
1 83 FunFam G3DSA:3.40.30.10:FF:000018 Glutaredoxin
4 82 NCBIfam TIGR02181 glutaredoxin 3
4 82 InterPro IPR011900 Glutaredoxin, GrxC
3 82 PANTHER PTHR45694 GLUTAREDOXIN 2
3 76 CDD cd03418 GRX_GRXb_1_3_like
3 76 InterPro IPR011900 Glutaredoxin, GrxC
1 83 ProSiteProfiles PS51354 Glutaredoxin domain profile.
4 22 PRINTS PR00160 Glutaredoxin signature
4 22 InterPro IPR014025 Glutaredoxin subgroup
46 59 PRINTS PR00160 Glutaredoxin signature
46 59 InterPro IPR014025 Glutaredoxin subgroup
60 73 PRINTS PR00160 Glutaredoxin signature
60 73 InterPro IPR014025 Glutaredoxin subgroup
1 83 SUPERFAMILY SSF52833 Thioredoxin-like
1 83 InterPro IPR036249 Thioredoxin-like superfamily

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

3D visualization script Full viewer

No pockets are loaded yet for the displayed AlphaFold model AF_A0A0H3GYR4 structure. Run experimental pocket backfill to show FPocket/P2Rank overlays on this structure.

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Structural evidence

0 + 2

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry Method Resolution Chain Coverage Links Status
AlphaFold AF_A0A0H3GYR4
AlphaFold full sequence Viewing
ColabFold KP13_00211
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

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.

Show only:
Ligand Source crystal UniProt (homolog) MW · LogP · TPSA Lipinski PAINS SMILES
CAC Q5NHD0 137.0 Da LogP -0.52 TPSA 40.1 ✓ Ro5 ✓ Clean C[As](=O)(C)[O-]
GDS A8MJH2 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 A0A1W6I4R7 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

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.