Protein profile

KP13_00850

2Fe-2S ferredoxin

Genome: KpKP13

Gene: AHE43214.1 fdx Structure source: AlphaFold + ColabFold UniProt A0A0H3GWP7
Amino acids 111
Annotations 6
Features 23
PDB binders 1
Druggability 0.563

Overview

Basic information about this protein and its source genome.

Accession
KP13_00850
Gene
AHE43214.1 fdx
Status
annotated
Amino acids
111
Structure source
AlphaFold + ColabFold

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
41.121
Human E-value
5e-14
Gut microbiome off-target
hit
Essential (DEG)
Y
DEG identity (%)
91.892
DEG E-value
4.15e-73
Localization
Cytoplasmic
ColabFold pLDDT
95.9

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 0.563
Structure A0A0H3GWP7
Pocket Pocket 1
P2Rank
Structure A0A0H3GWP7
Pocket No pockets
ColabFold model
FPocket 0.47 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 235 / 4744 genomes with a hit
Normalized 0.05

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

6 GO

Gene Ontology (GO)

6
  • 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: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:0140647 A electron transport chain in which one or more electron carriers operate to transfer electrons from donors to a cytochrome P450 protein or domain. Electron carriers operating in this chain include FAD-containing flavoproteins or domains, FMN domains, ferredoxins and cytochrome b5. The reduced cytochrome P450 functions as the terminal oxidase and participates in a wide range of biochemical pathways.
  • GO:0051536 Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms.
  • GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
  • GO:0046872 Binding to a metal ion.

Sequence Features

Domain/signature hits from InterPro and related databases.

23 records
Show feature table
Start End DB Term Name
1 111 Gene3D G3DSA:3.10.20.30 -
1 111 InterPro IPR012675 Beta-grasp domain superfamily
42 52 ProSitePatterns PS00814 Adrenodoxin family, iron-sulfur binding region signature.
42 52 InterPro IPR018298 Adrenodoxin, iron-sulphur binding site
2 111 NCBIfam TIGR02007 ferredoxin, 2Fe-2S type, ISC system
2 111 InterPro IPR011536 Ferredoxin 2Fe-2S type, proteobacteria
42 52 PRINTS PR00355 Adrenodoxin signature
42 52 InterPro IPR001055 Adrenodoxin
60 74 PRINTS PR00355 Adrenodoxin signature
60 74 InterPro IPR001055 Adrenodoxin
83 91 PRINTS PR00355 Adrenodoxin signature
83 91 InterPro IPR001055 Adrenodoxin
1 111 FunFam G3DSA:3.10.20.30:FF:000008 Ferredoxin, 2Fe-2S type, ISC system
4 109 SUPERFAMILY SSF54292 2Fe-2S ferredoxin-like
4 109 InterPro IPR036010 2Fe-2S ferredoxin-like superfamily
14 92 Pfam PF00111 2Fe-2S iron-sulfur cluster binding domain
14 92 InterPro IPR001041 2Fe-2S ferredoxin-type iron-sulfur binding domain
2 104 ProSiteProfiles PS51085 2Fe-2S ferredoxin-type iron-sulfur binding domain profile.
2 104 InterPro IPR001041 2Fe-2S ferredoxin-type iron-sulfur binding domain
18 108 PANTHER PTHR23426 FERREDOXIN/ADRENODOXIN
18 108 InterPro IPR001055 Adrenodoxin
14 99 CDD cd00207 fer2
14 99 InterPro IPR001041 2Fe-2S ferredoxin-type iron-sulfur binding domain

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

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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_A0A0H3GWP7
AlphaFold full sequence Viewing
ColabFold KP13_00850
ColabFold full sequence Loaded
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET Sticks Spheres Surfaces Druggability Labels Zoom Positions
1 0.563
5 0.004
2 0.001
3 0.0

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.

1 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
FES P0A9R4 175.8 Da LogP 1.29 TPSA 0.0 ✓ Ro5 ✓ Clean S1[Fe]S[Fe]1

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.