Protein profile

PA2298

oxidoreductase

Genome: NC_002516.2

Gene: PA2298 Structure source: AlphaFold UniProt Q9I1H7
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Amino acids 574
Annotations 6
Features 19
PDB binders 14
Druggability 0.792

Overview

Basic information about this protein and its source genome.

Accession
PA2298
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA2298
Status
annotated
Amino acids
574
Structure source
AlphaFold
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: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:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2. GO:0000104 Catalysis of the reaction: succinate + acceptor = fumarate + reduced acceptor. 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: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.

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
Gut microbiome off-target
hit
Essential (DEG)
N
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 0.792
Structure –
Pocket –

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:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
  • 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:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.
  • GO:0000104 Catalysis of the reaction: succinate + acceptor = fumarate + reduced acceptor.
  • 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: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.

19 records
Show feature table
Start End DB Term Name
10 29 PRINTS PR00368 FAD-dependent pyridine nucleotide reductase signature
355 377 PRINTS PR00368 FAD-dependent pyridine nucleotide reductase signature
4 407 SUPERFAMILY SSF51905 FAD/NAD(P)-binding domain
4 407 InterPro IPR036188 FAD/NAD(P)-binding domain superfamily
9 378 Pfam PF00890 FAD binding domain
9 378 InterPro IPR003953 FAD-dependent oxidoreductase 2, FAD binding domain
316 553 Gene3D G3DSA:3.50.50.60 -
316 553 InterPro IPR036188 FAD/NAD(P)-binding domain superfamily
1 274 Gene3D G3DSA:3.50.50.60 -
1 274 InterPro IPR036188 FAD/NAD(P)-binding domain superfamily
440 542 Pfam PF02910 Fumarate reductase flavoprotein C-term
440 542 InterPro IPR015939 Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal
1 561 PIRSF PIRSF000171 SDHA_APRA_LASPO
370 377 PRINTS PR00411 Pyridine nucleotide disulphide reductase class-I signature
9 31 PRINTS PR00411 Pyridine nucleotide disulphide reductase class-I signature
2 554 PANTHER PTHR11632 SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT
2 554 InterPro IPR030664 FAD-dependent oxidoreductase SdhA/FrdA/AprA
425 552 SUPERFAMILY SSF46977 Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal domain
425 552 InterPro IPR037099 Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal domain superfamily

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 PA2298
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 0.792

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.

64 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
ADX
2FJA
O28603 427.3 Da LogP -2.04 TPSA 229.4 1 viol. ✓ Clean c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…
AT5
2ACZ
P0AC41 366.2 Da LogP 2.79 TPSA 88.6 ✓ Ro5 ✓ Clean C[C@@H](C[C@H](C)C(=O)C1=C(C(=C(NC1=O)OC)OC)O)[…
CBE
2WDQ
P0AC41 235.3 Da LogP 2.62 TPSA 38.3 ✓ Ro5 ✓ Clean CC1=C(SCCO1)C(=O)Nc2ccccc2
CDN
1NEK
P0AC41 1151.5 Da LogP 14.77 TPSA 249.6 4 viol. ✓ Clean CCCCCCCCCCCCCCC(O)O[C@H](COC(CCCCC)O)CO[P@@](=O…
DNT
1NEN
P0AC41 282.3 Da LogP 3.89 TPSA 106.5 ✓ Ro5 ✓ Clean CCCCCC(C)c1cc(cc(c1O)[N+](=O)[O-])[N+](=O)[O-]
EPH
1NEK
P0AC41 709.9 Da LogP 10.16 TPSA 134.4 2 viol. ✓ Clean CCCC=CCC=CCCCCCCCC(=O)O[C@H](COC(=O)CCCCCCC=CCC…
F3S
1NEK
P0AC41 295.8 Da LogP 2.59 TPSA 0.0 ✓ Ro5 ✓ Clean S1[Fe]2S[Fe]3[S]2[Fe]1S3
FES
1NEK
P0AC41 175.8 Da LogP 1.29 TPSA 0.0 ✓ Ro5 ✓ Clean S1[Fe]S[Fe]1
OAA
1NEK
P0AC41 131.1 Da LogP -2.22 TPSA 94.5 ✓ Ro5 ✓ Clean C(C(=O)C(=O)O)C(=O)[O-]
PCI
2WDR
P0AC41 266.3 Da LogP 4.66 TPSA 20.2 ✓ Ro5 ✓ Clean c1(c(c(c(c(c1Cl)Cl)Cl)Cl)Cl)O
SFD
2FJB
O28603 867.6 Da LogP -2.88 TPSA 401.7 3 viol. ✓ Clean Cc1cc2c(cc1C)[N@](C3C(=O)NC(=O)N=C3N2C[C@@H]([C…
SIN
1KNP
P10902 118.1 Da LogP -0.06 TPSA 74.6 ✓ Ro5 ✓ Clean C(CC(=O)O)C(=O)O
TEO
2WDQ
P0AC41 132.1 Da LogP -3.14 TPSA 103.7 ✓ Ro5 ✓ Clean C(=C(\O)/[O-])\[C@H](C(=O)[O-])O
UQ2
1NEK
P0AC41 318.4 Da LogP 4.04 TPSA 52.6 ✓ Ro5 Alert CC1=C(C(=O)C(=C(C1=O)OC)OC)C\C=C(/C)\CCC=C(C)C

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.