Protein profile

PA0447

glutaryl-CoA dehydrogenase

Genome: NC_002516.2

Gene: gcdH PA0447 Structure source: AlphaFold UniProt Q9I671

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Amino acids 393

Annotations 8

Features 24

PDB binders 9

Druggability 0.737

Overview

Basic information about this protein and its source genome.

Accession: PA0447
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: gcdH PA0447
Status: annotated
Amino acids: 393
Structure source: AlphaFold

1.3.8.6

GO:0000062 Binding to a fatty-acyl-CoA, any derivative of coenzyme A in which the sulfhydryl group is in thiolester linkage with a fatty acyl group. 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:0004361 Catalysis of the reaction: glutaryl-CoA + 2 H+ + oxidized [electron-transfer flavoprotein] = (2E)-butenoyl-CoA + CO2 + reduced [electron-transfer flavoprotein]. 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:0046949 The chemical reactions and pathways resulting in the formation of a fatty-acyl-CoA, any derivative of coenzyme A in which the sulfhydryl group is in thiolester linkage with a fatty-acyl group. 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].

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 65.394
Human E-value: 0.0
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 0.737

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Enzyme Commission (EC)

1.3.8.6

Gene Ontology (GO)

GO:0000062 Binding to a fatty-acyl-CoA, any derivative of coenzyme A in which the sulfhydryl group is in thiolester linkage with a fatty acyl group.
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:0004361 Catalysis of the reaction: glutaryl-CoA + 2 H+ + oxidized [electron-transfer flavoprotein] = (2E)-butenoyl-CoA + CO2 + reduced [electron-transfer flavoprotein].
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:0046949 The chemical reactions and pathways resulting in the formation of a fatty-acyl-CoA, any derivative of coenzyme A in which the sulfhydryl group is in thiolester linkage with a fatty-acyl group.
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: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.

24 records

Show feature table

Start	End	DB	Term	Name
239	385	Pfam	PF00441	Acyl-CoA dehydrogenase, C-terminal domain
239	385	InterPro	IPR009075	Acyl-CoA dehydrogenase/oxidase C-terminal
241	393	FunFam	G3DSA:1.20.140.10:FF:000006	Glutaryl-CoA dehydrogenase, mitochondrial
243	390	SUPERFAMILY	SSF47203	Acyl-CoA dehydrogenase C-terminal domain-like
243	390	InterPro	IPR036250	Acyl-CoA dehydrogenase-like, C-terminal
136	227	Pfam	PF02770	Acyl-CoA dehydrogenase, middle domain
136	227	InterPro	IPR006091	Acyl-CoA oxidase/dehydrogenase, middle domain
15	94	PIRSF	PIRSF016578	PIGM
149	391	PIRSF	PIRSF016578	PIGM
135	238	FunFam	G3DSA:2.40.110.10:FF:000008	Glutaryl-CoA dehydrogenase, mitochondrial
20	132	Pfam	PF02771	Acyl-CoA dehydrogenase, N-terminal domain
20	132	InterPro	IPR013786	Acyl-CoA dehydrogenase/oxidase, N-terminal
7	392	CDD	cd01151	GCD
135	239	Gene3D	G3DSA:2.40.110.10	-
135	239	InterPro	IPR046373	Acyl-CoA oxidase/dehydrogenase, middle domain superfamily
345	364	ProSitePatterns	PS00073	Acyl-CoA dehydrogenases signature 2.
345	364	InterPro	IPR006089	Acyl-CoA dehydrogenase, conserved site
3	392	PANTHER	PTHR42807	GLUTARYL-COA DEHYDROGENASE, MITOCHONDRIAL
7	238	SUPERFAMILY	SSF56645	Acyl-CoA dehydrogenase NM domain-like
7	238	InterPro	IPR009100	Acyl-CoA dehydrogenase/oxidase, N-terminal and middle domain superfamily
1	133	Gene3D	G3DSA:1.10.540.10	-
1	133	InterPro	IPR037069	Acyl-CoA dehydrogenase/oxidase, N-terminal domain superfamily
1	133	FunFam	G3DSA:1.10.540.10:FF:000003	glutaryl-CoA dehydrogenase, mitochondrial
240	393	Gene3D	G3DSA:1.20.140.10	-

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 PA0447	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				0.737

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.

59 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
341	3EON	Q3JP94	144.1 Da LogP 1.46 TPSA 20.2	✓ Ro5	✓ Clean	`c1c(cc(cc1F)F)CO`
4NI	2R0M	Q92947	133.1 Da LogP 0.13 TPSA 80.4	✓ Ro5	✓ Clean	`C(CC(=O)O)C[N+](=O)[O-]`
54D	3D6B	Q3JP94	142.2 Da LogP 1.53 TPSA 26.3	✓ Ro5	✓ Clean	`COC(=O)c1cccs1`
COS	4L1F	D2RL84	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	3SF6	A0QV68	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…`
NBC	1SIR	Q92947	882.6 Da LogP -1.28 TPSA 406.8	3 viol.	✓ Clean	`CC(C)(CO[P@](=O)(O)O[P@@](=O)(O)OC[C@@H]1[C@H](…`
QQQ	3GNC	Q3JP94	240.3 Da LogP 1.86 TPSA 72.2	✓ Ro5	✓ Clean	`CC(C)n1c2ccccc2nc1S(=O)(=O)O`
TGC	2R0N	Q92947	899.7 Da LogP -1.52 TPSA 400.9	3 viol.	✓ Clean	`CC(C)(CO[P@](=O)(O)O[P@](=O)(O)OC[C@@H]1[C@H]([…`
UFO	3GQT	Q3JP94	191.3 Da LogP 1.03 TPSA 32.5	✓ Ro5	✓ Clean	`CN1CCN(c2c1ccc(c2)CN)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
ZINC169362726	1.000	240.3 Da LogP 1.86 TPSA 72.2	✓ Ro5	✓ Clean	`CC(C)n1c(S(=O)(=O)O)nc2ccccc21`
ZINC6366355	0.757	254.3 Da LogP 2.25 TPSA 72.2	✓ Ro5	✓ Clean	`CC[C@@H](C)n1c(S(=O)(=O)O)nc2ccccc21`
ZINC6366387	0.757	254.3 Da LogP 2.25 TPSA 72.2	✓ Ro5	✓ Clean	`CC[C@H](C)n1c(S(=O)(=O)O)nc2ccccc21`
ZINC100840031	0.737	302.4 Da LogP 2.89 TPSA 72.2	✓ Ro5	✓ Clean	`C[C@@H](c1ccccc1)n1c(S(=O)(=O)O)nc2ccccc21`
ZINC100840033	0.737	302.4 Da LogP 2.89 TPSA 72.2	✓ Ro5	✓ Clean	`C[C@H](c1ccccc1)n1c(S(=O)(=O)O)nc2ccccc21`
ZINC2528585	0.682	205.0 Da LogP 2.08 TPSA 20.2	✓ Ro5	✓ Clean	`OCc1cc(F)cc(Br)c1`
ZINC96028520	0.682	252.0 Da LogP 1.92 TPSA 20.2	✓ Ro5	✓ Clean	`OCc1cc(F)cc(I)c1`
ZINC240611	0.667	262.3 Da LogP 2.75 TPSA 52.6	✓ Ro5	✓ Clean	`COC(=O)c1ccc(OC(=O)c2cccs2)cc1`
ZINC38213092	0.656	246.3 Da LogP 2.77 TPSA 43.4	✓ Ro5	✓ Clean	`COC(=O)c1ccccc1C(=O)c1cccs1`
ZINC364025	0.647	262.3 Da LogP 2.75 TPSA 52.6	✓ Ro5	✓ Clean	`COC(=O)c1ccccc1OC(=O)c1cccs1`
ZINC40005117	0.647	267.3 Da LogP 2.85 TPSA 55.4	✓ Ro5	✓ Clean	`COC(=O)c1ccc(NC(=O)c2cccs2)s1`
ZINC169354629	0.639	212.2 Da LogP 0.82 TPSA 72.2	✓ Ro5	✓ Clean	`Cn1c(S(=O)(=O)O)nc2ccccc21`
ZINC169363486	0.625	254.3 Da LogP 1.94 TPSA 72.2	✓ Ro5	✓ Clean	`CC(C)Cn1c(S(=O)(=O)O)nc2ccccc21`
ZINC477393	0.625	234.3 Da LogP 2.98 TPSA 35.5	✓ Ro5	✓ Clean	`COc1ccc(OC(=O)c2cccs2)cc1`
ZINC323538	0.621	330.4 Da LogP 4.25 TPSA 52.6	✓ Ro5	✓ Clean	`O=C(Oc1ccc(OC(=O)c2cccs2)cc1)c1cccs1`
ZINC4717843	0.621	282.3 Da LogP 2.82 TPSA 52.6	✓ Ro5	✓ Clean	`O=C(OCCOC(=O)c1cccs1)c1cccs1`
ZINC85394422	0.618	236.2 Da LogP 2.36 TPSA 56.5	✓ Ro5	✓ Clean	`COC(=O)c1ccc(C(=O)c2cccs2)o1`
ZINC12138041	0.611	262.3 Da LogP 2.75 TPSA 52.6	✓ Ro5	✓ Clean	`COC(=O)c1cccc(OC(=O)c2cccs2)c1`
ZINC471712	0.611	276.3 Da LogP 2.89 TPSA 52.6	✓ Ro5	✓ Clean	`COC(=O)c1ccc(COC(=O)c2cccs2)cc1`
ZINC6143005	0.610	268.3 Da LogP 2.33 TPSA 72.2	✓ Ro5	✓ Clean	`CC(C)CCn1c(S(=O)(=O)O)nc2ccccc21`
ZINC338538	0.606	234.3 Da LogP 2.98 TPSA 35.5	✓ Ro5	✓ Clean	`COc1ccccc1OC(=O)c1cccs1`
ZINC6792942	0.606	224.3 Da LogP 3.26 TPSA 26.3	✓ Ro5	✓ Clean	`COC(=O)c1ccc(-c2cccs2)s1`
ZINC123866	0.600	261.3 Da LogP 2.79 TPSA 55.4	✓ Ro5	✓ Clean	`COC(=O)c1ccc(NC(=O)c2cccs2)cc1`
ZINC47204238	0.600	220.2 Da LogP 3.12 TPSA 20.2	✓ Ro5	✓ Clean	`OCc1cc(F)cc(-c2ccc(F)cc2)c1`
ZINC2512239	0.595	213.2 Da LogP -0.00 TPSA 98.2	✓ Ro5	✓ Clean	`Nn1c(S(=O)(=O)O)nc2ccccc21`
ZINC2361993	0.590	226.3 Da LogP 1.30 TPSA 72.2	✓ Ro5	✓ Clean	`CCn1c(S(=O)(=O)O)nc2ccccc21`
ZINC101676	0.583	319.3 Da LogP 2.57 TPSA 81.7	✓ Ro5	✓ Clean	`COC(=O)c1cc(NC(=O)c2cccs2)cc(C(=O)OC)c1`
ZINC115925	0.583	267.3 Da LogP 2.85 TPSA 55.4	✓ Ro5	✓ Clean	`COC(=O)c1ccsc1NC(=O)c1cccs1`
ZINC185415062	0.583	228.3 Da LogP 1.86 TPSA 52.6	✓ Ro5	✓ Clean	`COC(=O)C[C@@H](C)OC(=O)c1cccs1`
ZINC4204227	0.583	220.2 Da LogP 3.12 TPSA 20.2	✓ Ro5	✓ Clean	`OCc1ccc(-c2cc(F)cc(F)c2)cc1`
ZINC47228	0.583	261.3 Da LogP 2.79 TPSA 55.4	✓ Ro5	✓ Clean	`COC(=O)c1ccccc1NC(=O)c1cccs1`
ZINC80421	0.583	267.3 Da LogP 2.85 TPSA 55.4	✓ Ro5	✓ Clean	`COC(=O)c1sccc1NC(=O)c1cccs1`
ZINC6467726	0.581	268.3 Da LogP 2.33 TPSA 72.2	✓ Ro5	✓ Clean	`CC[C@@H](C)Cn1c(S(=O)(=O)O)nc2ccccc21`
ZINC6467727	0.581	268.3 Da LogP 2.33 TPSA 72.2	✓ Ro5	✓ Clean	`CC[C@H](C)Cn1c(S(=O)(=O)O)nc2ccccc21`
ZINC140759	0.581	204.2 Da LogP 2.97 TPSA 26.3	✓ Ro5	✓ Clean	`O=C(Oc1ccccc1)c1cccs1`
ZINC40860	0.579	341.2 Da LogP 3.52 TPSA 52.6	✓ Ro5	✓ Clean	`COC(=O)c1cc(Br)ccc1OC(=O)c1cccs1`
ZINC9112134	0.579	268.3 Da LogP 2.24 TPSA 68.3	✓ Ro5	✓ Clean	`COC(=O)c1cnc(NC(=O)c2cccs2)s1`
ZINC9314311	0.579	292.3 Da LogP 2.76 TPSA 61.8	✓ Ro5	✓ Clean	`COC(=O)c1ccc(OC(=O)c2cccs2)c(OC)c1`
ZINC1710767	0.577	222.3 Da LogP 2.88 TPSA 34.1	✓ Ro5	Alert	`O=C(C(=O)c1cccs1)c1cccs1`
ZINC100003546	0.576	212.2 Da LogP 1.06 TPSA 60.4	✓ Ro5	✓ Clean	`COC(=O)C(=O)CC(=O)c1cccs1`
ZINC1644075	0.576	218.3 Da LogP 3.28 TPSA 26.3	✓ Ro5	✓ Clean	`Cc1ccc(OC(=O)c2cccs2)cc1`
ZINC348328	0.576	251.3 Da LogP 3.39 TPSA 38.7	✓ Ro5	✓ Clean	`C/C(=N/OC(=O)c1cccs1)c1cccs1`
ZINC169340469	0.575	240.3 Da LogP 1.69 TPSA 72.2	✓ Ro5	✓ Clean	`CCCn1c(S(=O)(=O)O)nc2ccccc21`
ZINC100477669	0.571	236.3 Da LogP 3.27 TPSA 34.1	✓ Ro5	✓ Clean	`O=C(CC(=O)c1cccs1)c1cccs1`
ZINC107289449	0.564	204.2 Da LogP 2.32 TPSA 55.1	✓ Ro5	✓ Clean	`CC(C)n1c(C(=O)O)nc2ccccc21`
ZINC12652603	0.564	331.4 Da LogP 1.71 TPSA 89.5	✓ Ro5	✓ Clean	`COC(=O)c1sccc1S(=O)(=O)NC(=O)c1cccs1`
ZINC4115370	0.564	274.3 Da LogP 2.27 TPSA 72.2	✓ Ro5	✓ Clean	`O=S(=O)(O)c1nc2ccccc2n1-c1ccccc1`
ZINC53944090	0.564	202.3 Da LogP 2.82 TPSA 34.9	✓ Ro5	✓ Clean	`CC(=O)c1nc2ccccc2n1C(C)C`
ZINC323545	0.563	330.4 Da LogP 4.25 TPSA 52.6	✓ Ro5	✓ Clean	`O=C(Oc1cccc(OC(=O)c2cccs2)c1)c1cccs1`
ZINC3319525	0.563	358.4 Da LogP 4.52 TPSA 52.6	✓ Ro5	✓ Clean	`O=C(OCc1ccc(COC(=O)c2cccs2)cc1)c1cccs1`

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.