Protein profile
VK055_4866
glycerol-3-phosphate dehydrogenase, anaerobic, Csubunit
Genome: KpATCC43816
Overview
Basic information about this protein and its source genome.
- Accession
- VK055_4866
- Gene
- glpC AIK83393.1
- Status
- annotated
- Amino acids
- 392
- Structure source
- AlphaFold + ColabFold
Target profile
Computed evidence for target prioritization.
- Human off-target
- No hit
- Human identity (%)
- 0.0
- Gut microbiome off-target
- hit
- Essential (DEG)
- N
- DEG identity (%)
- 24.065
- Localization
- CytoplasmicMembrane
- ColabFold pLDDT
- 95.71
Selected Druggability evidence
AlphaFold / UniProt modelSelected 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.
Sequence
Primary amino-acid sequence viewer.
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Gene Ontology (GO)
8- GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
- GO:0051536 Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms.
- GO:0009061 The enzymatic release of energy from inorganic and organic compounds (especially carbohydrates and fats) which uses compounds other than oxygen (e.g. nitrate, sulfate) as the terminal electron acceptor.
- GO:0009331 An enzyme complex that catalyzes the oxidation of sn-glycerol 3-phosphate to dihydroxyacetone phosphate, with concurrent reduction of flavin adenine dinucleotide (FAD) to FADH2. In E. coli, the complex is either a GlpA-GlpB-GlpC heterotrimer that functions in anaerobic conditions, or a GlpD homodimer that functions in aerobic conditions.
- GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
- GO:0051539 Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands.
- GO:0046872 Binding to a metal ion.
- 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.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 6 | 69 | InterPro | IPR017896 | 4Fe-4S ferredoxin-type, iron-sulphur binding domain |
| 56 | 67 | ProSitePatterns | PS00198 | 4Fe-4S ferredoxin-type iron-sulfur binding region signature. |
| 56 | 67 | InterPro | IPR017900 | 4Fe-4S ferredoxin, iron-sulphur binding, conserved site |
| 45 | 70 | ProSiteProfiles | PS51379 | 4Fe-4S ferredoxin-type iron-sulfur binding domain profile. |
| 45 | 70 | InterPro | IPR017896 | 4Fe-4S ferredoxin-type, iron-sulphur binding domain |
| 6 | 83 | SUPERFAMILY | SSF46548 | alpha-helical ferredoxin |
| 289 | 372 | Pfam | PF02754 | Cysteine-rich domain |
| 289 | 372 | InterPro | IPR004017 | Cysteine-rich domain |
| 163 | 245 | Pfam | PF02754 | Cysteine-rich domain |
| 163 | 245 | InterPro | IPR004017 | Cysteine-rich domain |
| 6 | 69 | Pfam | PF13183 | 4Fe-4S dicluster domain |
| 3 | 89 | Gene3D | G3DSA:1.10.1060.10 | - |
| 3 | 89 | InterPro | IPR009051 | Alpha-helical ferredoxin |
| 1 | 29 | ProSiteProfiles | PS51379 | 4Fe-4S ferredoxin-type iron-sulfur binding domain profile. |
| 1 | 29 | InterPro | IPR017896 | 4Fe-4S ferredoxin-type, iron-sulphur binding domain |
| 3 | 89 | FunFam | G3DSA:1.10.1060.10:FF:000008 | Glycerol-3-phosphate dehydrogenase, anaerobic, C subunit |
| 3 | 391 | PANTHER | PTHR32479 | GLYCOLATE OXIDASE IRON-SULFUR SUBUNIT |
| 3 | 391 | NCBIfam | TIGR03379 | anaerobic glycerol-3-phosphate dehydrogenase subunit GlpC |
| 3 | 391 | InterPro | IPR017753 | Glycerol-3-phosphate dehydrogenase, GlpC subunit |
3D Structure
Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.
Loading 3D structure...
Structural evidence
0 + 2Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold
AF_A0A0H3GSZ6
|
AlphaFold | — | — | full sequence | — | Viewing |
|
ColabFold
VK055_4866
|
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 |
|---|---|---|---|---|---|---|---|
| 6 | 0.995 |
Pockets (P2RANK)
Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).
| P2RANK | Sticks | Spheres | Surfaces | Score | Probability | Labels | Zoom | Positions |
|---|---|---|---|---|---|---|---|---|
| 1 | 36.03 | 0.954 | ||||||
| 2 | 3.77 | 0.145 | ||||||
| 3 | 3.52 | 0.129 | ||||||
| 4 | 3.43 | 0.124 | ||||||
| 5 | 1.67 | 0.028 |
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 |
|---|---|---|---|---|---|---|---|
| 8 | 0.997 |
Pockets (P2RANK)
Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).
| P2RANK | Sticks | Spheres | Surfaces | Score | Probability | Labels | Zoom | Positions |
|---|---|---|---|---|---|---|---|---|
| 1 | 34.49 | 0.95 | ||||||
| 2 | 3.8 | 0.147 | ||||||
| 3 | 3.5 | 0.128 | ||||||
| 4 | 3.24 | 0.112 | ||||||
| 5 | 2.38 | 0.063 |