Overview
Basic information about this protein and its source genome.
- Accession
- KP13_00984
- Gene
- AHE43486.1 nuoK
- Status
- annotated
- Amino acids
- 100
- 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)
- Y
- DEG identity (%)
- 95.0
- DEG E-value
- 4.29e-63
- Localization
- CytoplasmicMembrane
- ColabFold pLDDT
- 95.84
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.
Enzyme Commission (EC)
1Gene Ontology (GO)
6- GO:0042773 The transfer of electrons through a series of electron donors and acceptors, generating energy that is ultimately used for synthesis of ATP.
- GO:0016651 Catalysis of an oxidation-reduction (redox) reaction in which NADH or NADPH acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor.
- GO:0030964 An integral membrane complex that possesses NADH oxidoreductase activity. The complex is one of the components of the electron transport chain. It catalyzes the transfer of a pair of electrons from NADH to a quinone.
- 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:0050136 Catalysis of the reaction: NADH + H+ + a quinone = NAD+ + a quinol.
- GO:0048038 Binding to a quinone, any member of a class of diketones derivable from aromatic compounds by conversion of two CH groups into CO groups with any necessary rearrangement of double bonds.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 82 | 100 | Phobius | CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm. |
| 2 | 100 | Hamap | MF_01456 | NAD(P)H-quinone oxidoreductase subunit 4L, chloroplastic [ndhE]. |
| 2 | 100 | InterPro | IPR001133 | NADH-ubiquinone oxidoreductase chain 4L/K |
| 1 | 100 | Gene3D | G3DSA:1.10.287.3510 | - |
| 6 | 24 | Phobius | TRANSMEMBRANE | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 1 | 100 | FunFam | G3DSA:1.10.287.3510:FF:000001 | NADH-quinone oxidoreductase subunit K |
| 8 | 95 | Pfam | PF00420 | NADH-ubiquinone/plastoquinone oxidoreductase chain 4L |
| 8 | 95 | InterPro | IPR039428 | NADH-ubiquinone oxidoreductase chain 4L/Mnh complex subunit C1-like |
| 25 | 30 | Phobius | CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm. |
| 5 | 97 | PANTHER | PTHR11434 | NADH-UBIQUINONE OXIDOREDUCTASE SUBUNIT ND4L |
| 5 | 97 | InterPro | IPR001133 | NADH-ubiquinone oxidoreductase chain 4L/K |
| 1 | 5 | Phobius | NON_CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. |
| 31 | 54 | Phobius | TRANSMEMBRANE | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 4 | 23 | TMHMM | TMhelix | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 28 | 50 | TMHMM | TMhelix | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 55 | 59 | Phobius | NON_CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. |
| 60 | 81 | Phobius | TRANSMEMBRANE | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 60 | 82 | TMHMM | TMhelix | Region of a membrane-bound protein predicted to be embedded in the membrane. |
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_A0A0H3H106
|
AlphaFold | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_00984
|
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 |
|---|---|---|---|---|---|---|---|
| 7 | 0.566 | ||||||
| 2 | 0.286 |
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 |
|---|---|---|---|---|---|---|---|
| 7 | 0.698 | ||||||
| 8 | 0.308 | ||||||
| 9 | 0.279 | ||||||
| 1 | 0.257 |