Protein profile

PA0879

acyl-CoA dehydrogenase

Genome: NC_002516.2

Gene: PA0879 Structure source: AlphaFold UniProt Q9I566

Export view

Amino acids 386

Annotations 5

Features 23

PDB binders 4

Druggability 0.856

Overview

Basic information about this protein and its source genome.

Accession: PA0879
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA0879
Status: annotated
Amino acids: 386
Structure source: AlphaFold

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0003995 Catalysis of the reaction: a 2,3-saturated acyl-CoA + H+ oxidized [electron-transfer flavoprotein] = a (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]. 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:0033539 A fatty acid beta-oxidation pathway in which the initial step of each oxidation cycle, which converts an acyl-CoA to a trans-2-enoyl-CoA, is catalyzed by acyl-CoA dehydrogenase; the electrons removed by oxidation pass through the respiratory chain to oxygen and leave H2O as the product. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and ends when only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively). GO:0016627 Catalysis of an oxidation-reduction (redox) reaction in which a CH-CH group acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 42.157
Human E-value: 2.97e-16
Gut microbiome off-target: hit
Essential (DEG): Y
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 0.856

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

5 GO

Gene Ontology (GO)

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0003995 Catalysis of the reaction: a 2,3-saturated acyl-CoA + H+ oxidized [electron-transfer flavoprotein] = a (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein].
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:0033539 A fatty acid beta-oxidation pathway in which the initial step of each oxidation cycle, which converts an acyl-CoA to a trans-2-enoyl-CoA, is catalyzed by acyl-CoA dehydrogenase; the electrons removed by oxidation pass through the respiratory chain to oxygen and leave H2O as the product. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and ends when only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively).
GO:0016627 Catalysis of an oxidation-reduction (redox) reaction in which a CH-CH group acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor.

Sequence Features

Domain/signature hits from InterPro and related databases.

23 records

Show feature table

Start	End	DB	Term	Name
120	235	Gene3D	G3DSA:2.40.110.10	-
120	235	InterPro	IPR046373	Acyl-CoA oxidase/dehydrogenase, middle domain superfamily
2	116	Gene3D	G3DSA:1.10.540.10	-
2	116	InterPro	IPR037069	Acyl-CoA dehydrogenase/oxidase, N-terminal domain superfamily
119	235	FunFam	G3DSA:2.40.110.10:FF:000014	Probable acyl-CoA dehydrogenase
236	382	FunFam	G3DSA:1.20.140.10:FF:000012	Acyl-CoA dehydrogenase fadE12
5	115	Pfam	PF02771	Acyl-CoA dehydrogenase, N-terminal domain
5	115	InterPro	IPR013786	Acyl-CoA dehydrogenase/oxidase, N-terminal
7	381	PANTHER	PTHR48083	MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED
1	116	FunFam	G3DSA:1.10.540.10:FF:000013	Acyl-CoA dehydrogenase
231	364	Pfam	PF00441	Acyl-CoA dehydrogenase, C-terminal domain
231	364	InterPro	IPR009075	Acyl-CoA dehydrogenase/oxidase C-terminal
338	357	ProSitePatterns	PS00073	Acyl-CoA dehydrogenases signature 2.
338	357	InterPro	IPR006089	Acyl-CoA dehydrogenase, conserved site
120	218	Pfam	PF02770	Acyl-CoA dehydrogenase, middle domain
120	218	InterPro	IPR006091	Acyl-CoA oxidase/dehydrogenase, middle domain
229	384	SUPERFAMILY	SSF47203	Acyl-CoA dehydrogenase C-terminal domain-like
229	384	InterPro	IPR036250	Acyl-CoA dehydrogenase-like, C-terminal
236	382	Gene3D	G3DSA:1.20.140.10	-
2	194	PIRSF	PIRSF016578	PIGM
235	383	PIRSF	PIRSF016578	PIGM
5	230	SUPERFAMILY	SSF56645	Acyl-CoA dehydrogenase NM domain-like
5	230	InterPro	IPR009100	Acyl-CoA dehydrogenase/oxidase, N-terminal and middle 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.

Loading 3D structure...

Legend High Medium Low

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 PA0879	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				0.856
13				0.598

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.

54 records

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, use Open crystal to inspect it in the structure viewer.

No PDB structure with a co-crystallized ligand found for this exact protein.

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.

Ligand	Source crystal	UniProt (homolog)	MW · LogP · TPSA	Lipinski	PAINS	SMILES
COS	5OL2	A0A031WJ47	799.6 Da LogP -1.02 TPSA 346.6	3 viol.	✓ Clean	`CC(C)(CO[P@](=O)(O)O[P@](=O)(O)OC[C@@H]1[C@H]([…`
FDA	4IV6	A0QTW7	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…`
GRA	3MPI	C3UVB0	881.6 Da LogP -1.08 TPSA 400.9	3 viol.	✓ Clean	`CC(C)(CO[P@](=O)(O)O[P@](=O)(O)OC[C@@H]1[C@H]([…`
PG5	4O5M	A0A0H3G544	178.2 Da LogP 0.31 TPSA 36.9	✓ Ro5	✓ Clean	`COCCOCCOCCOC`

Experimental bioactivity from ChEMBL measured directly on this protein. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL bioactivity data found for this exact protein.

Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL hits found through similar proteins.

Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).

Ligand	Tanimoto	MW · LogP · TPSA	Lipinski	PAINS	SMILES
ZINC1692489	1.000	222.3 Da LogP 0.33 TPSA 46.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOC`
ZINC4530388	1.000	266.3 Da LogP 0.35 TPSA 55.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOC`
ZINC5701172	1.000	310.4 Da LogP 0.36 TPSA 64.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOC`
ZINC5997861	1.000	398.5 Da LogP 0.40 TPSA 83.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOC`
ZINC34764844	0.733	206.3 Da LogP 1.09 TPSA 36.9	✓ Ro5	✓ Clean	`CCCOCCOCCOCCOC`
ZINC140264883	0.688	223.3 Da LogP -0.43 TPSA 72.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCON`
ZINC143705779	0.688	443.5 Da LogP -0.34 TPSA 118.3	1 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCON`
ZINC1580161	0.688	208.3 Da LogP -0.33 TPSA 57.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCO`
ZINC16052118	0.688	340.4 Da LogP -0.28 TPSA 84.8	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCO`
ZINC16052257	0.688	384.5 Da LogP -0.26 TPSA 94.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC33358855	0.688	207.3 Da LogP -0.36 TPSA 62.9	✓ Ro5	✓ Clean	`COCCOCCOCCOCCN`
ZINC34317654	0.688	472.6 Da LogP -0.23 TPSA 112.5	1 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC44076059	0.688	428.5 Da LogP -0.24 TPSA 103.3	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC44583772	0.688	356.5 Da LogP 0.66 TPSA 64.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCS`
ZINC5024003	0.688	251.3 Da LogP -0.34 TPSA 72.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCN`
ZINC5210101	0.688	252.3 Da LogP -0.31 TPSA 66.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCO`
ZINC575432090	0.688	355.4 Da LogP -0.38 TPSA 99.9	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCON`
ZINC575432265	0.688	399.5 Da LogP -0.36 TPSA 109.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCON`
ZINC5997860	0.688	296.4 Da LogP -0.29 TPSA 75.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCO`
ZINC71254558	0.688	444.6 Da LogP 0.70 TPSA 83.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC71254563	0.688	488.6 Da LogP 0.71 TPSA 92.3	1 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC80685077	0.688	427.5 Da LogP -0.28 TPSA 109.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCN`
ZINC83253927	0.688	400.5 Da LogP 0.68 TPSA 73.8	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC83253930	0.688	224.3 Da LogP 0.61 TPSA 36.9	✓ Ro5	✓ Clean	`COCCOCCOCCOCCS`
ZINC83253936	0.688	383.5 Da LogP -0.29 TPSA 99.9	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCN`
ZINC90556279	0.688	295.4 Da LogP -0.33 TPSA 81.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCN`
ZINC90556280	0.688	339.4 Da LogP -0.31 TPSA 90.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCN`
ZINC90556286	0.688	312.4 Da LogP 0.65 TPSA 55.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCS`
ZINC90556287	0.688	268.4 Da LogP 0.63 TPSA 46.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCS`
ZINC96503353	0.688	471.6 Da LogP -0.26 TPSA 118.3	1 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCN`
ZINC113456917	0.647	220.3 Da LogP 1.48 TPSA 36.9	✓ Ro5	✓ Clean	`CCCCOCCOCCOCCOC`
ZINC146934560	0.647	397.5 Da LogP -0.03 TPSA 85.9	✓ Ro5	✓ Clean	`COCCOCCOCCOCCNCCOCCOCCOCCOC`
ZINC218810670	0.647	308.4 Da LogP 1.52 TPSA 55.4	✓ Ro5	✓ Clean	`CCCCOCCOCCOCCOCCOCCOC`
ZINC33506597	0.647	309.4 Da LogP -0.06 TPSA 67.4	✓ Ro5	✓ Clean	`COCCOCCOCCNCCOCCOCCOC`
ZINC34303570	0.647	264.4 Da LogP 1.50 TPSA 46.2	✓ Ro5	✓ Clean	`CCCCOCCOCCOCCOCCOC`
ZINC3860567	0.647	323.4 Da LogP 0.28 TPSA 58.6	✓ Ro5	✓ Clean	`COCCOCCN(CCOCCOC)CCOCCOC`
ZINC5701149	0.647	221.3 Da LogP -0.10 TPSA 49.0	✓ Ro5	✓ Clean	`COCCOCCNCCOCCOC`
ZINC1083807034	0.611	207.5 Da LogP 2.02 TPSA 18.5	✓ Ro5	✓ Clean	`COCCOCC(Cl)(Cl)Cl`
ZINC1083807936	0.611	202.2 Da LogP 1.23 TPSA 27.7	✓ Ro5	✓ Clean	`COCCOCCOCC(F)(F)F`
ZINC115163232	0.611	222.3 Da LogP 0.07 TPSA 57.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCCO`
ZINC125689999	0.611	221.3 Da LogP 0.03 TPSA 62.9	✓ Ro5	✓ Clean	`COCCOCCOCCOCCCN`
ZINC2571901	0.611	204.3 Da LogP 0.87 TPSA 36.9	✓ Ro5	✓ Clean	`C=CCOCCOCCOCCOC`
ZINC258837490	0.611	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCCO`
ZINC4583025	0.611	234.3 Da LogP 0.84 TPSA 46.2	✓ Ro5	✓ Clean	`C=COCCOCCOCCOCCOC`
ZINC136908049	0.600	220.3 Da LogP 1.48 TPSA 36.9	✓ Ro5	✓ Clean	`COCCCOCCCOCCCOC`
ZINC1542984464	0.579	466.6 Da LogP 0.42 TPSA 92.3	✓ Ro5	✓ Clean	`C#CCOCCOCCOCCOCCOCCOCCOCCOCCOCCOC`
ZINC1596133	0.579	206.2 Da LogP 0.23 TPSA 54.0	✓ Ro5	✓ Clean	`COCCOCCOCCOC(C)=O`
ZINC33994361	0.579	222.2 Da LogP -0.23 TPSA 74.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCC(=O)O`
ZINC60215744	0.579	310.3 Da LogP -0.20 TPSA 92.7	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCC(=O)O`
ZINC83253938	0.579	412.5 Da LogP 0.22 TPSA 111.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCC(=O)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.