Target Pathogen

Overview

Basic information about this protein and its source genome.

Accession: PA4140
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA4140
Status: annotated
Amino acids: 597
Structure source: AlphaFold

GO

GO:0071949 Binding to the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes. 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:0022904 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 to generate a transmembrane electrochemical gradient. 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:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Gut microbiome off-target: hit
Essential (DEG): N
Localization: Unknown

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 0.749

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MHDLIQHADAFVGDPDQESGGLSRRSFLGKSATLGAVGLVAGWTPAFVIQPAEAAASSCPAPAGFPAGLELYRRAFRNWSGEIAADDLWSCAPRTNEEVLAVVNWAWQNGFKVRPRGMGHNWSPLLLKGGENCESRIVLVETSRYLTRVRIDAQGEFGLFSAQTGVTMEALLKQLERVKLGFVATPAPGDLTLGGVLAIDGHGTGIPAQGESRLPGQSYGSLSNSIVALTAVVWDGAAGQYVLKTFRRDDPACAPFLVHLGRAFIVEATLQAGVNKRMRCQSYVNIPASEMFAAAGSGGRTFDSFLQKSGRAEAIWFPFTDKPWLKVWTPTPRCPFGARAVNGPFNYPFSDNIPKALSDLLAAINTGHPELTPLLGKLQYDLVVGGMALTLGYDLWGWSKDLLLYIKPSTLRVTANGYAVLTRRRDVQRVINEFYLQYQTMVAAYRANGHYPMNGPVEIRVSGLDQPGESIVPGAQVPSLSAIRPRPDQPEWDTAIWLDILSLPGTPQANAFYHEFEAWLFDHFSGDYASLRVEWSKGWGYSPAAAWDEPTVVDQLVAQSLRQGLVADNDWDSAVRQLNEADPHRLFSSPLLDRLMP

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

5 GO

Gene Ontology (GO)

5

GO:0071949 Binding to the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
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:0022904 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 to generate a transmembrane electrochemical gradient.
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:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.

Sequence Features

Domain/signature hits from InterPro and related databases.

23 records

Show feature table

Start	End	DB	Term	Name
277	597	Pfam	PF09129	Cholesterol oxidase, substrate-binding
277	597	InterPro	IPR015213	Cholesterol oxidase, substrate-binding
1	56	ProSiteProfiles	PS51318	Twin arginine translocation (Tat) signal profile.
1	56	InterPro	IPR006311	Twin-arginine translocation pathway, signal sequence
548	597	Gene3D	G3DSA:1.10.45.10	-
548	597	InterPro	IPR016171	Vanillyl-alcohol oxidase, C-terminal subdomain 2
92	211	Pfam	PF01565	FAD binding domain
92	211	InterPro	IPR006094	FAD linked oxidase, N-terminal
277	597	SUPERFAMILY	SSF55103	FAD-linked oxidases, C-terminal domain
277	597	InterPro	IPR016164	FAD-linked oxidase-like, C-terminal
82	275	ProSiteProfiles	PS51387	PCMH-type FAD-binding domain profile.
82	275	InterPro	IPR016166	FAD-binding domain, PCMH-type
33	587	PANTHER	PTHR43716	D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL
62	271	SUPERFAMILY	SSF56176	FAD-binding/transporter-associated domain-like
62	271	InterPro	IPR036318	FAD-binding, type PCMH-like superfamily
70	146	Gene3D	G3DSA:3.30.43.10	-
70	146	InterPro	IPR016167	FAD-binding, type PCMH, subdomain 1
22	54	NCBIfam	TIGR01409	twin-arginine translocation signal domain
22	54	InterPro	IPR019546	Twin-arginine translocation pathway, signal sequence, bacterial/archaeal
275	547	Gene3D	G3DSA:3.40.462.10	-
275	547	InterPro	IPR016170	Cytokinin dehydrogenase, C-terminal domain superfamily
147	273	Gene3D	G3DSA:3.30.465.10	-
147	273	InterPro	IPR016169	FAD-binding, type PCMH, subdomain 2

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 PA4140	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				0.749
10				0.261

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.

1 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
CAC	1I19	Q7SID9	137.0 Da LogP -0.52 TPSA 40.1	✓ Ro5	✓ Clean	`C[As](=O)(C)[O-]`

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).

No virtual-screening candidates for this protein.

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.

PA4140