Protein profile

PA4130

sulfite/nitrite reductase

Genome: NC_002516.2

Gene: PA4130 Structure source: AlphaFold UniProt Q9HWQ1

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Amino acids 557

Annotations 7

Features 27

PDB binders 3

Druggability 0.73

Overview

Basic information about this protein and its source genome.

Accession: PA4130
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA4130
Status: annotated
Amino acids: 557
Structure source: AlphaFold

GO:0009337 A multisubunit iron flavoprotein, which in yeast is composed of 2 alpha and 2 beta subunits. Catalyzes the reduction of sulfite to sulfide. GO:0051539 Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands. GO:0020037 Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring. GO:0046872 Binding to a metal ion. 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:0000103 The pathways by which inorganic sulfate is processed and incorporated into sulfated compounds.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
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 0.73

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MYQYDEYDQALVSERVAQFRDQIARRLDGELSEEEFLPLRLQNGLYLQKHAYMLRVAIPYGTLSAPQLRALAHVARHYDRGYGHFTTRQNIQFNWIELEQVGDILEHLAGAQMHAIQTSGNCVRNITTEAFAGVAADEWTDPRPLAEILRQWSTVNPEFLFLPRKFKIALSSAVEDRAAVQMHDIGLYLYRHPDAGELRLRVLVGGGLGRTPMLGQVIRDDLPWQHLLSYVEAILRVYNRYGRRDNKYKARIKILVKALGIEAFAREVEEEWQHLRDGPAQLTAEECQRVAERFVLPRYLPPADGELAYGSARAADPAFARWASRNVQAHKVPGYASVVLSTKPGASAPPGDVTAEQMERVADWAERYGFGEIRVAHEQNLVLPDVRLENLHALWREACAAGLGTPNQGLLSDIIACPGGDYCALANAKSIPIAQGIQQRFEDLDHLHDIGELSLNISGCMNACGHHHIGNIGILGVDKSGSEWYQVTLGGAQGKDSALGKVIGPSFSAAEVPAVIERIVETFTDLRVGPERFIDTFNRVGLEPFKARVYARMEEPA

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

7 GO

Gene Ontology (GO)

GO:0009337 A multisubunit iron flavoprotein, which in yeast is composed of 2 alpha and 2 beta subunits. Catalyzes the reduction of sulfite to sulfide.
GO:0051539 Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands.
GO:0020037 Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring.
GO:0046872 Binding to a metal ion.
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:0000103 The pathways by which inorganic sulfate is processed and incorporated into sulfated compounds.
GO:0051536 Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms.

Sequence Features

Domain/signature hits from InterPro and related databases.

27 records

Show feature table

Start	End	DB	Term	Name
119	318	Gene3D	G3DSA:3.30.413.10	Sulfite Reductase Hemoprotein, domain 1
119	318	InterPro	IPR045854	Nitrite and sulphite reductase 4Fe-4S domain-like superfamily
119	274	Pfam	PF01077	Nitrite and sulphite reductase 4Fe-4S domain
119	274	InterPro	IPR006067	Nitrite/sulphite reductase 4Fe-4S domain
1	126	SUPERFAMILY	SSF55124	Nitrite/Sulfite reductase N-terminal domain-like
1	126	InterPro	IPR036136	Nitrite/Sulfite reductase ferredoxin-like domain superfamily
412	430	PRINTS	PR00397	Sirohaem Fe-binding site signature
412	430	InterPro	IPR006066	Nitrite/sulphite reductase iron-sulphur/sirohaem-binding site
458	476	PRINTS	PR00397	Sirohaem Fe-binding site signature
458	476	InterPro	IPR006066	Nitrite/sulphite reductase iron-sulphur/sirohaem-binding site
409	556	Gene3D	G3DSA:3.30.413.10	Sulfite Reductase Hemoprotein, domain 1
409	556	InterPro	IPR045854	Nitrite and sulphite reductase 4Fe-4S domain-like superfamily
19	550	PANTHER	PTHR11493	SULFITE REDUCTASE [NADPH] SUBUNIT BETA-RELATED
19	550	InterPro	IPR045169	Nitrite and sulphite reductase 4Fe-4S domain containing protein
253	423	SUPERFAMILY	SSF55124	Nitrite/Sulfite reductase N-terminal domain-like
253	423	InterPro	IPR036136	Nitrite/Sulfite reductase ferredoxin-like domain superfamily
414	555	Pfam	PF01077	Nitrite and sulphite reductase 4Fe-4S domain
414	555	InterPro	IPR006067	Nitrite/sulphite reductase 4Fe-4S domain
52	393	Gene3D	G3DSA:3.90.480.10	Sulfite Reductase Hemoprotein;Domain 2
120	286	SUPERFAMILY	SSF56014	Nitrite and sulphite reductase 4Fe-4S domain-like
120	286	InterPro	IPR045854	Nitrite and sulphite reductase 4Fe-4S domain-like superfamily
347	398	Pfam	PF03460	Nitrite/Sulfite reductase ferredoxin-like half domain
347	398	InterPro	IPR005117	Nitrite/Sulfite reductase ferredoxin-like domain
49	109	Pfam	PF03460	Nitrite/Sulfite reductase ferredoxin-like half domain
49	109	InterPro	IPR005117	Nitrite/Sulfite reductase ferredoxin-like domain
409	554	SUPERFAMILY	SSF56014	Nitrite and sulphite reductase 4Fe-4S domain-like
409	554	InterPro	IPR045854	Nitrite and sulphite reductase 4Fe-4S domain-like superfamily

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

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Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold PA4130	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				0.73
14				0.372

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.

53 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
FES	5H8Y	O23813	175.8 Da LogP 1.29 TPSA 0.0	✓ Ro5	✓ Clean	`S1[Fe]S[Fe]1`
HOA	3VKT	Q76KB0	33.0 Da LogP -0.67 TPSA 46.2	✓ Ro5	✓ Clean	`NO`
NO2	3VKP	Q76KB0	46.0 Da LogP 0.25 TPSA 52.5	✓ Ro5	✓ Clean	`N(=O)[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
ZINC403598	0.800	273.3 Da LogP 2.14 TPSA 92.8	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(Oc2ccc(O)cc2)cc1)C(=O)O`
ZINC403599	0.800	273.3 Da LogP 2.14 TPSA 92.8	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(Oc2ccc(O)cc2)cc1)C(=O)O`
ZINC39351856	0.741	328.4 Da LogP 1.26 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(-c2ccc(C[C@H](N)C(=O)O)cc2)cc1)C…`
ZINC32333	0.690	244.1 Da LogP 1.40 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(Br)cc1)C(=O)O`
ZINC32334	0.690	244.1 Da LogP 1.40 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(Br)cc1)C(=O)O`
ZINC3679925	0.690	291.1 Da LogP 1.25 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(I)cc1)C(=O)O`
ZINC391104	0.690	291.1 Da LogP 1.25 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(I)cc1)C(=O)O`
ZINC4202286	0.690	209.2 Da LogP 0.34 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(C(=O)O)cc1)C(=O)O`
ZINC4202287	0.690	209.2 Da LogP 0.34 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(C(=O)O)cc1)C(=O)O`
ZINC6092920	0.690	223.2 Da LogP 0.27 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(CC(=O)O)cc1)C(=O)O`
ZINC6506146	0.690	223.2 Da LogP 0.27 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(CC(=O)O)cc1)C(=O)O`
ZINC34319489	0.688	231.3 Da LogP 1.50 TPSA 83.5	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc2cc(O)ccc2c1)C(=O)O`
ZINC34319490	0.688	231.3 Da LogP 1.50 TPSA 83.5	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc2cc(O)ccc2c1)C(=O)O`
ZINC2512061	0.677	360.4 Da LogP 0.67 TPSA 167.1	1 viol.	✓ Clean	`N[C@@H](Cc1ccc(O)c(-c2cc(C[C@H](N)C(=O)O)ccc2O)…`
ZINC6091882	0.677	360.4 Da LogP 0.67 TPSA 167.1	1 viol.	✓ Clean	`N[C@@H](Cc1ccc(O)c(-c2cc(C[C@@H](N)C(=O)O)ccc2O…`
ZINC6091894	0.677	360.4 Da LogP 0.67 TPSA 167.1	1 viol.	✓ Clean	`N[C@H](Cc1ccc(O)c(-c2cc(C[C@@H](N)C(=O)O)ccc2O)…`
ZINC113264413	0.667	317.4 Da LogP 3.98 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(-c2ccc(-c3ccccc3)cc2)cc1)C(=O)O`
ZINC113264415	0.667	317.4 Da LogP 3.98 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(-c2ccc(-c3ccccc3)cc2)cc1)C(=O)O`
ZINC14982778	0.667	207.2 Da LogP 0.84 TPSA 80.4	✓ Ro5	✓ Clean	`CC(=O)c1ccc(C[C@@H](N)C(=O)O)cc1`
ZINC14982780	0.667	207.2 Da LogP 0.84 TPSA 80.4	✓ Ro5	✓ Clean	`CC(=O)c1ccc(C[C@H](N)C(=O)O)cc1`
ZINC1569734	0.667	238.2 Da LogP -0.54 TPSA 112.6	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(O)cc1)C(=O)NCC(=O)O`
ZINC2244337	0.667	241.3 Da LogP 2.31 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(-c2ccccc2)cc1)C(=O)O`
ZINC2244338	0.667	241.3 Da LogP 2.31 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(-c2ccccc2)cc1)C(=O)O`
ZINC2505456	0.667	210.2 Da LogP 0.72 TPSA 94.8	✓ Ro5	✓ Clean	`O=C(O)C(Cc1ccc(O)cc1)C(=O)O`
ZINC2575475	0.667	238.2 Da LogP -0.54 TPSA 112.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(O)cc1)C(=O)NCC(=O)O`
ZINC2575618	0.667	208.2 Da LogP -0.26 TPSA 106.4	✓ Ro5	✓ Clean	`NC(=O)c1ccc(C[C@H](N)C(=O)O)cc1`
ZINC4241956	0.667	208.2 Da LogP -0.26 TPSA 106.4	✓ Ro5	✓ Clean	`NC(=O)c1ccc(C[C@@H](N)C(=O)O)cc1`
ZINC2004481	0.647	344.4 Da LogP 0.78 TPSA 132.9	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](Cc1ccc(O)cc1)…`
ZINC116924508	0.645	215.2 Da LogP 1.58 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(C(F)F)cc1)C(=O)O`
ZINC116924543	0.645	215.2 Da LogP 1.58 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(C(F)F)cc1)C(=O)O`
ZINC2385595	0.645	207.3 Da LogP 1.76 TPSA 63.3	✓ Ro5	✓ Clean	`CC(C)c1ccc(C[C@H](N)C(=O)O)cc1`
ZINC2392305	0.645	221.3 Da LogP 1.94 TPSA 63.3	✓ Ro5	✓ Clean	`CC(C)(C)c1ccc(C[C@H](N)C(=O)O)cc1`
ZINC2392306	0.645	221.3 Da LogP 1.94 TPSA 63.3	✓ Ro5	✓ Clean	`CC(C)(C)c1ccc(C[C@@H](N)C(=O)O)cc1`
ZINC3679865	0.645	207.3 Da LogP 1.76 TPSA 63.3	✓ Ro5	✓ Clean	`CC(C)c1ccc(C[C@@H](N)C(=O)O)cc1`
ZINC44283754	0.645	207.3 Da LogP 1.59 TPSA 63.3	✓ Ro5	✓ Clean	`CCCc1ccc(C[C@H](N)C(=O)O)cc1`
ZINC44283756	0.645	207.3 Da LogP 1.59 TPSA 63.3	✓ Ro5	✓ Clean	`CCCc1ccc(C[C@@H](N)C(=O)O)cc1`
ZINC44284738	0.645	255.3 Da LogP 2.62 TPSA 63.3	✓ Ro5	✓ Clean	`Cc1ccc(-c2ccc(C[C@H](N)C(=O)O)cc2)cc1`
ZINC44284740	0.645	255.3 Da LogP 2.62 TPSA 63.3	✓ Ro5	✓ Clean	`Cc1ccc(-c2ccc(C[C@@H](N)C(=O)O)cc2)cc1`
ZINC4763192	0.636	271.3 Da LogP 2.01 TPSA 72.5	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(O)cc1)C(=O)OCc1ccccc1`
ZINC4763195	0.636	271.3 Da LogP 2.01 TPSA 72.5	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(O)cc1)C(=O)OCc1ccccc1`
ZINC2566273	0.629	252.3 Da LogP -0.15 TPSA 112.7	✓ Ro5	✓ Clean	`C[C@H](NC(=O)[C@@H](N)Cc1ccc(O)cc1)C(=O)O`
ZINC2566279	0.629	252.3 Da LogP -0.15 TPSA 112.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(O)cc1)C(=O)NCCC(=O)O`
ZINC3590784	0.629	252.3 Da LogP -0.15 TPSA 112.7	✓ Ro5	✓ Clean	`C[C@@H](NC(=O)[C@@H](N)Cc1ccc(O)cc1)C(=O)O`
ZINC4787311	0.629	252.3 Da LogP -0.15 TPSA 112.7	✓ Ro5	✓ Clean	`C[C@H](NC(=O)[C@H](N)Cc1ccc(O)cc1)C(=O)O`
ZINC4787313	0.629	252.3 Da LogP -0.15 TPSA 112.7	✓ Ro5	✓ Clean	`C[C@@H](NC(=O)[C@H](N)Cc1ccc(O)cc1)C(=O)O`
ZINC20112424	0.625	259.2 Da LogP 0.32 TPSA 120.9	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(CP(=O)(O)O)cc1)C(=O)O`
ZINC2149429	0.625	233.2 Da LogP 1.66 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(C(F)(F)F)cc1)C(=O)O`
ZINC2149431	0.625	233.2 Da LogP 1.66 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(C(F)(F)F)cc1)C(=O)O`
ZINC3679854	0.625	211.3 Da LogP 1.36 TPSA 63.3	✓ Ro5	✓ Clean	`CSc1ccc(C[C@@H](N)C(=O)O)cc1`
ZINC44284605	0.625	275.7 Da LogP 2.96 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(-c2ccc(Cl)cc2)cc1)C(=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.