Protein profile

PA3875

respiratory nitrate reductase subunit alpha

Genome: NC_002516.2

Gene: PA3875 GUL26_00750 CAZ10_29350 narG Structure source: AlphaFold UniProt G3XCX1 UniProt O54043
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Amino acids 1261
Annotations 13
Features 30
PDB binders 17
Druggability 0.507

Overview

Basic information about this protein and its source genome.

Accession
PA3875
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA3875 GUL26_00750 CAZ10_29350 narG
Status
annotated
Amino acids
1261
Structure source
AlphaFold
EC
1.7.5.1
GO
GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. GO:0009325 An enzyme complex that catalyzes the formation of nitrate from nitrite with the concomitant reduction of an acceptor. 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:0043546 Binding to a molybdopterin cofactor (Moco), essential for the catalytic activity of some enzymes, e.g. sulfite oxidase, xanthine dehydrogenase, and aldehyde oxidase. The cofactor consists of a mononuclear molybdenum (Mo-molybdopterin) or tungsten ion (W-molybdopterin) coordinated by one or two molybdopterin ligands.

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
Gut microbiome off-target
hit
Essential (DEG)
Y
Localization
CytoplasmicMembrane

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 0.507
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 12 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

12
  • GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
  • GO:0009325 An enzyme complex that catalyzes the formation of nitrate from nitrite with the concomitant reduction of an acceptor.
  • 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:0043546 Binding to a molybdopterin cofactor (Moco), essential for the catalytic activity of some enzymes, e.g. sulfite oxidase, xanthine dehydrogenase, and aldehyde oxidase. The cofactor consists of a mononuclear molybdenum (Mo-molybdopterin) or tungsten ion (W-molybdopterin) coordinated by one or two molybdopterin ligands.
  • GO:0160182 Catalysis of the reaction: a quinol + nitrate = a quinone + H2O + nitrite.
  • GO:0019645 A process in which a series of electron carriers operate together to transfer electrons from donors such as NADH and FADH2 to any of several different terminal electron acceptors other than oxygen to generate a transmembrane electrochemical gradient.
  • GO:0042128 The nitrogen metabolic process that encompasses the uptake of nitrate from the environment and reduction to ammonia, and results in the incorporation of nitrogen derived from nitrate into cellular substances.
  • 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:0008940 Catalysis of the reaction: nitrite + acceptor = nitrate + reduced acceptor.
  • GO:0042126 The chemical reactions and pathways involving nitrates, inorganic or organic salts and esters of nitric acid.

Sequence Features

Domain/signature hits from InterPro and related databases.

30 records
Show feature table
Start End DB Term Name
44 1248 Gene3D G3DSA:3.40.50.12440 -
5 1232 PANTHER PTHR43105 RESPIRATORY NITRATE REDUCTASE
1131 1158 ProSitePatterns PS00932 Prokaryotic molybdopterin oxidoreductases signature 3.
1131 1158 InterPro IPR006655 Molybdopterin oxidoreductase, prokaryotic, conserved site
43 105 SMART SM00926 Molybdop_Fe4S4_2
43 105 InterPro IPR006963 Molybdopterin oxidoreductase, 4Fe-4S domain
4 1076 SUPERFAMILY SSF53706 Formate dehydrogenase/DMSO reductase, domains 1-3
48 66 ProSitePatterns PS00551 Prokaryotic molybdopterin oxidoreductases signature 1.
48 66 InterPro IPR027467 Molybdopterin oxidoreductase, molybdopterin cofactor binding site
2 43 Gene3D G3DSA:4.10.1200.10 nitrate reductase tail
2 43 InterPro IPR044906 Nitrate reductase, alpha subunit, N-terminal domain superfamily
2 1241 NCBIfam TIGR01580 nitrate reductase subunit alpha
2 1241 InterPro IPR006468 Nitrate reductase, alpha subunit
44 1242 FunFam G3DSA:3.40.50.12440:FF:000001 Nitrate reductase subunit alpha
3 40 Pfam PF14710 Respiratory nitrate reductase alpha N-terminal
3 40 InterPro IPR028189 Nitrate reductase, alpha subunit, N-terminal
1085 1241 SUPERFAMILY SSF50692 ADC-like
1085 1241 InterPro IPR009010 Aspartate decarboxylase-like domain superfamily
780 797 ProSitePatterns PS00490 Prokaryotic molybdopterin oxidoreductases signature 2.
780 797 InterPro IPR006655 Molybdopterin oxidoreductase, prokaryotic, conserved site
108 836 Pfam PF00384 Molybdopterin oxidoreductase
108 836 InterPro IPR006656 Molybdopterin oxidoreductase
43 107 ProSiteProfiles PS51669 Prokaryotic molybdopterin oxidoreductases 4Fe-4S domain profile.
43 107 InterPro IPR006963 Molybdopterin oxidoreductase, 4Fe-4S domain
1092 1232 CDD cd02776 MopB_CT_Nitrate-R-NarG-like
1092 1232 InterPro IPR037943 Nitrate reductase alpha subunit-like, MopB domain
1093 1208 Pfam PF01568 Molydopterin dinucleotide binding domain
1093 1208 InterPro IPR006657 Molybdopterin dinucleotide-binding domain
43 837 CDD cd02750 MopB_Nitrate-R-NarG-like
2 43 FunFam G3DSA:4.10.1200.10:FF:000001 Respiratory nitrate reductase subunit alpha

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 PA3875
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
9 0.507
10 0.339
36 0.228

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.

67 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
2MO
1E61
Q52675 127.9 Da LogP -0.24 TPSA 34.1 ✓ Ro5 ✓ Clean O=[Mo]=O
3PH
1Q16
P09152 705.0 Da LogP 12.07 TPSA 119.4 2 viol. ✓ Clean CCCCCCCCCCCCCCCCCC(=O)OC[C@H](COP(=O)(O)O)OC(=O…
4MO
2DMR
Q52675 95.9 Da LogP -0.00 TPSA 0.0 ✓ Ro5 ✓ Clean [Mo+4]
6MO
1DMR
Q52675 95.9 Da LogP -0.00 TPSA 0.0 ✓ Ro5 ✓ Clean [Mo+6]
6WO
1E18
Q52675 199.8 Da LogP -0.12 TPSA 17.1 ✓ Ro5 ✓ Clean O=[W+4]
AGA
1Q16
P09152 455.5 Da LogP 1.85 TPSA 151.7 ✓ Ro5 ✓ Clean CCCCCCCC(=O)O[C@H](COC(=O)CCCC)COP(=O)([O-])OC[…
BSY
5CHC
G8QM55 128.0 Da LogP -2.25 TPSA 60.4 ✓ Ro5 ✓ Clean O[Se](=O)[O-]
BTT
4V4E
P80563 142.1 Da LogP 0.51 TPSA 80.9 ✓ Ro5 Alert c1c(c(cc(c1O)O)O)O
F3S
7B04
Q1PZD8 295.8 Da LogP 2.59 TPSA 0.0 ✓ Ro5 ✓ Clean S1[Fe]2S[Fe]3[S]2[Fe]1S3
MD1
7B04
Q1PZD8 740.6 Da LogP -2.13 TPSA 358.0 3 viol. ✓ Clean c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O…
MGD
4V4C
P80563 740.6 Da LogP -2.06 TPSA 346.6 3 viol. ✓ Clean c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@@](=…
MO
7B04
Q1PZD8 95.9 Da LogP -0.00 TPSA 0.0 ✓ Ro5 ✓ Clean [Mo]
O
1DMR
Q52675 18.0 Da LogP -0.82 TPSA 31.5 ✓ Ro5 ✓ Clean O
PCI
1Y4Z
P09152 266.3 Da LogP 4.66 TPSA 20.2 ✓ Ro5 ✓ Clean c1(c(c(c(c(c1Cl)Cl)Cl)Cl)Cl)O
PGD
1DMR
Q52675 738.6 Da LogP -2.97 TPSA 343.0 3 viol. ✓ Clean c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@@](=…
PYG
4V4D
P80563 126.1 Da LogP 0.80 TPSA 60.7 ✓ Ro5 Alert c1cc(c(c(c1)O)O)O
SO2
2DMR
Q52675 64.1 Da LogP -0.67 TPSA 34.1 ✓ Ro5 ✓ Clean O=S=O

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.