Target Pathogen

Overview

Basic information about this protein and its source genome.

Accession: PA3392
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA3392 nosZ
Status: annotated
Amino acids: 636
Structure source: AlphaFold

EC

1.7.2.4

GO

GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. GO:0042597 The region between the inner (cytoplasmic) and outer membrane (Gram-negative Bacteria) or cytoplasmic membrane and cell wall (Fungi and Gram-positive Bacteria). GO:0005509 Binding to a calcium ion (Ca2+). GO:0005507 Binding to a copper (Cu) ion. GO:0004129 Catalysis of the reaction: 4 Fe(II)-[cytochrome c] + O2 + 8 H+(in) = 4 Fe(III)-[cytochrome c] + 2 H2O + 4 H+(out). GO:0050304 Catalysis of the reaction: H2O + 2 cytochrome c + nitrogen = 2 reduced cytochrome c + nitrous oxide.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Gut microbiome off-target: hit
Essential (DEG): Y
Localization: Periplasmic

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 0.351

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Enzyme Commission (EC)

1

1.7.2.4

Gene Ontology (GO)

8

GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
GO:0042597 The region between the inner (cytoplasmic) and outer membrane (Gram-negative Bacteria) or cytoplasmic membrane and cell wall (Fungi and Gram-positive Bacteria).
GO:0005509 Binding to a calcium ion (Ca2+).
GO:0005507 Binding to a copper (Cu) ion.
GO:0004129 Catalysis of the reaction: 4 Fe(II)-[cytochrome c] + O2 + 8 H+(in) = 4 Fe(III)-[cytochrome c] + 2 H2O + 4 H+(out).
GO:0050304 Catalysis of the reaction: H2O + 2 cytochrome c + nitrogen = 2 reduced cytochrome c + nitrous oxide.
GO:0019333 The reduction of nitrate to dinitrogen by four reduction reactions: nitrate reduced to nitrite, then to nitric oxide, then to nitrous oxide, and finally to dinitrogen.
GO:0005515 Binding to a protein.

Sequence Features

Domain/signature hits from InterPro and related databases.

35 records

Show feature table

Start	End	DB	Term	Name
507	634	SUPERFAMILY	SSF49503	Cupredoxins
507	634	InterPro	IPR008972	Cupredoxin
1	49	ProSiteProfiles	PS51318	Twin arginine translocation (Tat) signal profile.
1	49	InterPro	IPR006311	Twin-arginine translocation pathway, signal sequence
537	636	ProSiteProfiles	PS50857	Cytochrome oxidase subunit II copper A binding domain profile.
537	636	InterPro	IPR002429	Cytochrome c oxidase subunit II-like C-terminal
576	627	Pfam	PF00116	Cytochrome C oxidase subunit II, periplasmic domain
576	627	InterPro	IPR002429	Cytochrome c oxidase subunit II-like C-terminal
2	635	Hamap	MF_00716	Nitrous-oxide reductase [nosZ].
2	635	InterPro	IPR023644	Nitrous-oxide reductase
422	492	Pfam	PF18764	Nitrous oxide reductase propeller repeat
422	492	InterPro	IPR041114	Nitrous oxide reductase, propeller repeat 1
15	42	NCBIfam	TIGR01409	twin-arginine translocation signal domain
15	42	InterPro	IPR019546	Twin-arginine translocation pathway, signal sequence, bacterial/archaeal
541	634	CDD	cd04223	N2OR_C
541	634	InterPro	IPR034205	Nitrous-oxide reductase, C-terminal
516	635	FunFam	G3DSA:2.60.40.420:FF:000095	Nitrous-oxide reductase
579	627	ProSitePatterns	PS00078	CO II and nitrous oxide reductase dinuclear copper centers signature.
579	627	InterPro	IPR001505	Copper centre Cu(A)
56	515	Gene3D	G3DSA:2.130.10.10	-
56	515	InterPro	IPR015943	WD40/YVTN repeat-like-containing domain superfamily
20	43	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
1	635	PANTHER	PTHR42838	CYTOCHROME C OXIDASE SUBUNIT II
56	515	FunFam	G3DSA:2.130.10.10:FF:001102	Nitrous-oxide reductase
1	19	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
169	239	Pfam	PF18793	Nitrous oxide reductase propeller repeat 2
169	239	InterPro	IPR041142	Nitrous oxide reductase, propeller repeat 2
516	634	Gene3D	G3DSA:2.60.40.420	-
516	634	InterPro	IPR008972	Cupredoxin
60	504	SUPERFAMILY	SSF50974	Nitrous oxide reductase, N-terminal domain
60	504	InterPro	IPR011045	Nitrous oxide reductase, N-terminal
20	42	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
44	636	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
15	634	NCBIfam	TIGR04244	TAT-dependent nitrous-oxide reductase
15	634	InterPro	IPR023644	Nitrous-oxide reductase

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 PA3392	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
2				0.351
7				0.295
1				0.221

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
B3P	6RKZ	P19573	282.3 Da LogP -4.01 TPSA 145.4	1 viol.	✓ Clean	`C(CNC(CO)(CO)CO)CNC(CO)(CO)CO`
BU3	5I5M	Q12M27	90.1 Da LogP -0.25 TPSA 40.5	✓ Ro5	✓ Clean	`C[C@H]([C@@H](C)O)O`
CUA	3SBP	P19573	127.1 Da LogP -0.01 TPSA 0.0	✓ Ro5	✓ Clean	`[Cu][Cu]`
CUK	3SBP	P19573	318.3 Da LogP 1.29 TPSA 0.0	✓ Ro5	✓ Clean	`S1[Cu]S([Cu]1)([Cu])[Cu]`
CUZ	6RKZ	P19573	286.3 Da LogP 0.64 TPSA 0.0	✓ Ro5	✓ Clean	`S123[Cu]4[Cu]15[Cu]24[Cu]35`
N2O	3SBR	P19573	44.0 Da LogP 0.34 TPSA 51.2	✓ Ro5	✓ Clean	`N#[N+][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).

Ligand	Tanimoto	MW · LogP · TPSA	Lipinski	PAINS	SMILES
ZINC4521259	1.000	282.3 Da LogP -4.01 TPSA 145.4	1 viol.	✓ Clean	`OCC(CO)(CO)NCCCNC(CO)(CO)CO`
ZINC115591405	0.636	373.6 Da LogP 4.55 TPSA 72.7	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCCCCNC(CO)(CO)CO`
ZINC115591837	0.636	317.5 Da LogP 2.99 TPSA 72.7	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCNC(CO)(CO)CO`
ZINC143575268	0.636	289.5 Da LogP 2.21 TPSA 72.7	✓ Ro5	✓ Clean	`CCCCCCCCCCCCNC(CO)(CO)CO`
ZINC2322313	0.636	233.4 Da LogP 0.65 TPSA 72.7	✓ Ro5	✓ Clean	`CCCCCCCCNC(CO)(CO)CO`
ZINC97996983	0.636	345.6 Da LogP 3.77 TPSA 72.7	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCCNC(CO)(CO)CO`
ZINC1611594	0.583	243.3 Da LogP -2.43 TPSA 127.1	✓ Ro5	✓ Clean	`O=S(=O)(O)CCCNC(CO)(CO)CO`
ZINC5273895	0.583	257.3 Da LogP -2.04 TPSA 127.1	✓ Ro5	✓ Clean	`O=S(=O)(O)CCCCNC(CO)(CO)CO`
ZINC1530141	0.500	229.3 Da LogP -2.82 TPSA 127.1	✓ Ro5	✓ Clean	`O=S(=O)(O)CCNC(CO)(CO)CO`

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.

PA3392