Protein profile

PA2994

Na(+)-translocating NADH-quinone reductase subunit F

Genome: NC_002516.2

Gene: PA2994 nqrF Structure source: AlphaFold UniProt Q9HZL1
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Amino acids 407
Annotations 10
Features 36
PDB binders 4
Druggability 0.675

Overview

Basic information about this protein and its source genome.

Accession
PA2994
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA2994 nqrF
Status
annotated
Amino acids
407
Structure source
AlphaFold
EC
7.2.1.1
GO
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: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: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: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. GO:0016655 Catalysis of an oxidation-reduction (redox) reaction in which NADH or NADPH acts as a hydrogen or electron donor and reduces a quinone or a similar acceptor molecule.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
24.537
Human E-value
1.6e-08
Gut microbiome off-target
hit
Essential (DEG)
N
Localization
Cytoplasmic

Selected Druggability evidence

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 0.675
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

MIGFEIFLAIGMFTAIVLGLVAIILVARAKLVSSGDVTIQINGEHSLTVPAGGKLLQTLAANNVFLSSACGGGGTCAQCKCVVVEGGGEMLPTEESHFTRRQAKEGWRLSCQTPVKQDMQIRVPEEVFGVKKWECTVESNPNVATFIKELTLRLPDGESVDFRAGGYVQLECPPHVVEYKDFDIQPEYRGDWDKFNMWRYVSKVDETVIRAYSMANYPEEKGVVKFNIRIASPPPGSDLPPGQMSSWVFNLKPGDKVTVYGPFGEFFAKDTEAEMVFIGGGAGMAPMRSHIFDQLRRLKSNRKISFWYGARSLREAFYTEEYDQLQAENPNFQWHLALSDPQPEDNWTGLTGFIHNVLFENYLKDHPAPEDCEFYMCGPPMMNAAVIKMLTDLGVERENILLDDFGG

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

9
  • 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: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: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: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.
  • GO:0016655 Catalysis of an oxidation-reduction (redox) reaction in which NADH or NADPH acts as a hydrogen or electron donor and reduces a quinone or a similar acceptor molecule.
  • GO:0006814 The directed movement of sodium ions (Na+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
  • 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.

Sequence Features

Domain/signature hits from InterPro and related databases.

36 records
Show feature table
Start End DB Term Name
6 27 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
275 393 FunFam G3DSA:3.40.50.80:FF:000014 Na(+)-translocating NADH-quinone reductase subunit F
7 29 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
36 126 Gene3D G3DSA:3.10.20.30 -
36 126 InterPro IPR012675 Beta-grasp domain superfamily
106 271 SUPERFAMILY SSF63380 Riboflavin synthase domain-like
106 271 InterPro IPR017938 Riboflavin synthase-like beta-barrel
40 125 SUPERFAMILY SSF54292 2Fe-2S ferredoxin-like
40 125 InterPro IPR036010 2Fe-2S ferredoxin-like superfamily
6 407 NCBIfam TIGR01941 NADH:ubiquinone reductase (Na(+)-transporting) subunit F
6 407 InterPro IPR010205 Na(+)-translocating NADH-quinone reductase subunit F
28 407 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
205 266 Pfam PF00970 Oxidoreductase FAD-binding domain
205 266 InterPro IPR008333 Flavoprotein pyridine nucleotide cytochrome reductase-like, FAD-binding domain
275 393 Gene3D G3DSA:3.40.50.80 -
275 393 InterPro IPR039261 Ferredoxin-NADP reductase (FNR), nucleotide-binding domain
1 5 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
1 407 PIRSF PIRSF000044 Cis_Diol_DH_RD
1 407 InterPro IPR010205 Na(+)-translocating NADH-quinone reductase subunit F
35 127 ProSiteProfiles PS51085 2Fe-2S ferredoxin-type iron-sulfur binding domain profile.
35 127 InterPro IPR001041 2Fe-2S ferredoxin-type iron-sulfur binding domain
26 407 PANTHER PTHR43644 NA(+)-TRANSLOCATING NADH-QUINONE REDUCTASE SUBUNIT
277 386 Pfam PF00175 Oxidoreductase NAD-binding domain
277 386 InterPro IPR001433 Oxidoreductase FAD/NAD(P)-binding
257 402 SUPERFAMILY SSF52343 Ferredoxin reductase-like, C-terminal NADP-linked domain
257 402 InterPro IPR039261 Ferredoxin-NADP reductase (FNR), nucleotide-binding domain
37 122 CDD cd00207 fer2
37 122 InterPro IPR001041 2Fe-2S ferredoxin-type iron-sulfur binding domain
4 407 Hamap MF_00430 Na(+)-translocating NADH-quinone reductase subunit F [nqrF].
4 407 InterPro IPR010205 Na(+)-translocating NADH-quinone reductase subunit F
127 264 Gene3D G3DSA:2.40.30.10 Translation factors
124 405 CDD cd06188 NADH_quinone_reductase
130 269 ProSiteProfiles PS51384 Ferredoxin reductase-type FAD binding domain profile.
130 269 InterPro IPR017927 FAD-binding domain, ferredoxin reductase-type
40 116 Pfam PF00111 2Fe-2S iron-sulfur cluster binding domain
40 116 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.

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Structural evidence

0 + 1

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

Entry Method Resolution Chain Coverage Links Status
AlphaFold PA2994
AlphaFold — — full sequence — Viewing
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 0.675
3 0.435

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.

35 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
A2P
1FNC
P00455 427.2 Da LogP -1.75 TPSA 232.6 2 viol. ✓ Clean c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…
BTB
4WQM
Q03304 209.2 Da LogP -3.01 TPSA 104.4 ✓ Ro5 ✓ Clean C(CO)N(CCO)C(CO)(CO)CO
FDA
1FNC
P00455 787.6 Da LogP -1.75 TPSA 363.3 3 viol. ✓ Clean Cc1cc2c(cc1C)N(C3=C(N2)C(=O)NC(=O)N3)C[C@@H]([C…
FES
5OGX
A0A076MZ01 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.