Protein profile

KP13_02397

Sulfite reductase [NADPH] hemoprotein beta-component

Genome: KpKP13

Gene: AHE42968.1 cysL Structure source: AlphaFold + ColabFold UniProt A0A0H3GXH1

Export view

Amino acids 570

Annotations 14

Features 32

PDB binders 5

Druggability 0.921

Overview

Basic information about this protein and its source genome.

Accession: KP13_02397
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE42968.1 cysL
Status: annotated
Amino acids: 570
Structure source: AlphaFold + ColabFold

1.8.1.2

GO:0004783 Catalysis of the reaction: hydrogen sulfide + 3 NADP+ + 3 H2O = sulfite + 3 NADPH + 3 H+. 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: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: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:0051536 Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms. GO:0050661 Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Human identity (%): 0.0
Gut microbiome off-target: hit
Essential (DEG): N
DEG identity (%): 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 95.48

Selected Druggability evidence

AlphaFold / UniProt model

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 0.921

Structure A0A0H3GXH1

Pocket Pocket 27

P2Rank 0.967

Structure A0A0H3GXH1

Pocket Pocket 1

ColabFold model

FPocket 0.895 · Pocket 14

P2Rank 0.951 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 151 / 4744 genomes with a hit

Normalized 0.032

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 13 GO

Enzyme Commission (EC)

1.8.1.2

Gene Ontology (GO)

GO:0004783 Catalysis of the reaction: hydrogen sulfide + 3 NADP+ + 3 H2O = sulfite + 3 NADPH + 3 H+.
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: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: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:0051536 Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms.
GO:0050661 Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH.
GO:0020037 Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring.
GO:0008652 The chemical reactions and pathways resulting in the formation of amino acids, organic acids containing one or more amino substituents.
GO:0046872 Binding to a metal ion.
GO:0050311 Catalysis of the reaction: hydrogen sulfide + 3 oxidized ferredoxin + 3 H2O = sulfite + 3 reduced ferredoxin.
GO:0019344 The chemical reactions and pathways resulting in the formation of L-cysteine, 2-amino-3-mercaptopropanoic acid.
GO:0070814 The chemical reactions and pathways resulting in the formation of hydrogen sulfide, H2S.
GO:0000103 The pathways by which inorganic sulfate is processed and incorporated into sulfated compounds.

Sequence Features

Domain/signature hits from InterPro and related databases.

32 records

Show feature table

Start	End	DB	Term	Name
10	570	Hamap	MF_01540	Sulfite reductase [NADPH] hemoprotein beta-component [cysI].
10	570	InterPro	IPR011786	Sulphite reductase (NADPH) hemoprotein, beta subunit
148	340	FunFam	G3DSA:3.30.413.10:FF:000004	Sulfite reductase [NADPH] hemoprotein beta-component
173	331	Pfam	PF01077	Nitrite and sulphite reductase 4Fe-4S domain
173	331	InterPro	IPR006067	Nitrite/sulphite reductase 4Fe-4S domain
150	344	SUPERFAMILY	SSF56014	Nitrite and sulphite reductase 4Fe-4S domain-like
150	344	InterPro	IPR045854	Nitrite and sulphite reductase 4Fe-4S domain-like superfamily
425	567	Gene3D	G3DSA:3.30.413.10	Sulfite Reductase Hemoprotein, domain 1
425	567	InterPro	IPR045854	Nitrite and sulphite reductase 4Fe-4S domain-like superfamily
477	493	ProSitePatterns	PS00365	Nitrite and sulfite reductases iron-sulfur/siroheme-binding site.
477	493	InterPro	IPR006066	Nitrite/sulphite reductase iron-sulphur/sirohaem-binding site
425	567	FunFam	G3DSA:3.30.413.10:FF:000003	Sulfite reductase [NADPH] hemoprotein beta-component
346	422	SUPERFAMILY	SSF55124	Nitrite/Sulfite reductase N-terminal domain-like
346	422	InterPro	IPR036136	Nitrite/Sulfite reductase ferredoxin-like domain superfamily
13	142	SUPERFAMILY	SSF55124	Nitrite/Sulfite reductase N-terminal domain-like
13	142	InterPro	IPR036136	Nitrite/Sulfite reductase ferredoxin-like domain superfamily
428	559	SUPERFAMILY	SSF56014	Nitrite and sulphite reductase 4Fe-4S domain-like
428	559	InterPro	IPR045854	Nitrite and sulphite reductase 4Fe-4S domain-like superfamily
353	416	Pfam	PF03460	Nitrite/Sulfite reductase ferredoxin-like half domain
353	416	InterPro	IPR005117	Nitrite/Sulfite reductase ferredoxin-like domain
81	138	Pfam	PF03460	Nitrite/Sulfite reductase ferredoxin-like half domain
81	138	InterPro	IPR005117	Nitrite/Sulfite reductase ferredoxin-like domain
12	565	PANTHER	PTHR11493	SULFITE REDUCTASE [NADPH] SUBUNIT BETA-RELATED
12	565	InterPro	IPR045169	Nitrite and sulphite reductase 4Fe-4S domain containing protein
429	447	PRINTS	PR00397	Sirohaem Fe-binding site signature
429	447	InterPro	IPR006066	Nitrite/sulphite reductase iron-sulphur/sirohaem-binding site
477	495	PRINTS	PR00397	Sirohaem Fe-binding site signature
477	495	InterPro	IPR006066	Nitrite/sulphite reductase iron-sulphur/sirohaem-binding site
19	558	NCBIfam	TIGR02041	assimilatory sulfite reductase (NADPH) hemoprotein subunit
19	558	InterPro	IPR011786	Sulphite reductase (NADPH) hemoprotein, beta subunit
148	340	Gene3D	G3DSA:3.30.413.10	Sulfite Reductase Hemoprotein, domain 1
148	340	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.

Loading 3D structure...

Legend High Medium Low

Structural evidence

0 + 2

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

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold AF_A0A0H3GXH1	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_02397	ColabFold	—	—	full sequence	—	Loaded

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
27				0.921

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Score	Probability
1	29.71	0.932
2	3.61	0.135
3	1.83	0.035
4	1.52	0.022
5	0.88	0.004

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
14				0.895

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Score	Probability
1	26.0	0.91
2	2.43	0.066
3	1.86	0.036
4	1.31	0.014

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.

55 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
CMO	5GEP	P17846	28.0 Da LogP -0.04 TPSA 19.9	✓ Ro5	✓ Clean	`[C-]#[O+]`
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	3GEO	P17846	46.0 Da LogP 0.25 TPSA 52.5	✓ Ro5	✓ Clean	`N(=O)[O-]`
SX	7GEP	P17846	48.1 Da LogP -0.34 TPSA 17.1	✓ Ro5	✓ Clean	`O=S`

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.