Target Pathogen

Overview

Basic information about this protein and its source genome.

Accession: PA4979
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA4979
Status: annotated
Amino acids: 386
Structure source: AlphaFold

GO

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: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 (%): 48.75
Human E-value: 2.94e-13
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 0.657

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MDFRLTQEQDMLVEAVRSFVEKELLPHEDDIDRADAVSPELAAQIRGKAIAAGFYAFNMPEEVGGGGLDYLSQALVERELSKVSWALHVFVARPSKILMACTGEQLGDYLLPCVQGEKTDCFALTEPGAGSDANSIKTRAVRDGDAFVINGSKHFISHAGHADFAIVFAVTDSYEHNGRKRNAVTAFLVDKGTPGMTVRRGPKCVSNRGYHTYEIFFDDCRVPASKVLGEVGKGWEVANAWLTAGRVMVAANCVGQAQRALDLSLRWAADRKQFGQPIGSYQGVSFKLADMATQIRAAELMTLHTAWKMDQGTMTDGEAGMAKLFASETLGKVADEAVQIFGGMGLMDEGPVERIWRNARIERIWEGTSEIQRHIVSRELLRPLLR

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

3 GO

Gene Ontology (GO)

3

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: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.

25 records

Show feature table

Start	End	DB	Term	Name
120	236	FunFam	G3DSA:2.40.110.10:FF:000002	Acyl-CoA dehydrogenase fadE12
339	358	ProSitePatterns	PS00073	Acyl-CoA dehydrogenases signature 2.
339	358	InterPro	IPR006089	Acyl-CoA dehydrogenase, conserved site
237	381	FunFam	G3DSA:1.20.140.10:FF:000001	Acyl-CoA dehydrogenase
3	381	PANTHER	PTHR43884	ACYL-COA DEHYDROGENASE
1	118	Gene3D	G3DSA:1.10.540.10	-
1	118	InterPro	IPR037069	Acyl-CoA dehydrogenase/oxidase, N-terminal domain superfamily
237	383	Gene3D	G3DSA:1.20.140.10	-
232	380	Pfam	PF00441	Acyl-CoA dehydrogenase, C-terminal domain
232	380	InterPro	IPR009075	Acyl-CoA dehydrogenase/oxidase C-terminal
121	220	Pfam	PF02770	Acyl-CoA dehydrogenase, middle domain
121	220	InterPro	IPR006091	Acyl-CoA oxidase/dehydrogenase, middle domain
123	135	ProSitePatterns	PS00072	Acyl-CoA dehydrogenases signature 1.
123	135	InterPro	IPR006089	Acyl-CoA dehydrogenase, conserved site
1	243	SUPERFAMILY	SSF56645	Acyl-CoA dehydrogenase NM domain-like
1	243	InterPro	IPR009100	Acyl-CoA dehydrogenase/oxidase, N-terminal and middle domain superfamily
6	117	Pfam	PF02771	Acyl-CoA dehydrogenase, N-terminal domain
6	117	InterPro	IPR013786	Acyl-CoA dehydrogenase/oxidase, N-terminal
230	382	SUPERFAMILY	SSF47203	Acyl-CoA dehydrogenase C-terminal domain-like
230	382	InterPro	IPR036250	Acyl-CoA dehydrogenase-like, C-terminal
235	383	PIRSF	PIRSF016578	PIGM
129	195	PIRSF	PIRSF016578	PIGM
3	88	PIRSF	PIRSF016578	PIGM
121	236	Gene3D	G3DSA:2.40.110.10	-
121	236	InterPro	IPR046373	Acyl-CoA oxidase/dehydrogenase, 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...

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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 PA4979	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
5				0.657
1				0.532

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.

15 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
CAA	1JQI	P15651	851.6 Da LogP -1.36 TPSA 380.7	3 viol.	✓ Clean	`CC(=O)CC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)CO[P…`
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	4N5F	B4EGC8	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…`

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
ZINC4228234	0.573	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC12360002	0.522	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12360703	0.522	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12503599	0.522	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC16546165	0.522	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@](=O)(O)OP(=O)(…`
ZINC31977053	0.522	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC4806433	0.522	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC53683898	0.522	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586019	0.522	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC8586020	0.522	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586021	0.522	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)OP(=O…`
ZINC8586022	0.522	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`

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.

PA4979