Protein profile

PA3814

cysteine desulfurase

Genome: NC_002516.2

Gene: iscS PA3814 Structure source: AlphaFold UniProt Q9HXI8

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Amino acids 404

Annotations 8

Features 19

PDB binders 11

Druggability 0.506

Overview

Basic information about this protein and its source genome.

Accession: PA3814
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: iscS PA3814
Status: annotated
Amino acids: 404
Structure source: AlphaFold

2.8.1.7

GO:1990221 A protein complex capable of cysteine desulfurase activity decomposing L-cysteine to L-alanine and sulfur. It belongs to a ubiquitous family of pyridoxal 5-phosphate (PLP)-dependent enzymes. GO:0051537 Binding to a 2 iron, 2 sulfur (2Fe-2S) cluster; this cluster consists of two iron atoms, with two inorganic sulfur atoms found between the irons and acting as bridging ligands. GO:0031071 Catalysis of the reaction: L-cysteine + [enzyme]-cysteine = L-alanine + [enzyme]-S-sulfanylcysteine. GO:0046872 Binding to a metal ion. GO:0030170 Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6. GO:0044571 The incorporation of two iron atoms and two sulfur atoms into an iron-sulfur cluster.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 72.0
Human E-value: 6.49e-31
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 0.506

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)

2.8.1.7

Gene Ontology (GO)

GO:1990221 A protein complex capable of cysteine desulfurase activity decomposing L-cysteine to L-alanine and sulfur. It belongs to a ubiquitous family of pyridoxal 5-phosphate (PLP)-dependent enzymes.
GO:0051537 Binding to a 2 iron, 2 sulfur (2Fe-2S) cluster; this cluster consists of two iron atoms, with two inorganic sulfur atoms found between the irons and acting as bridging ligands.
GO:0031071 Catalysis of the reaction: L-cysteine + [enzyme]-cysteine = L-alanine + [enzyme]-S-sulfanylcysteine.
GO:0046872 Binding to a metal ion.
GO:0030170 Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6.
GO:0044571 The incorporation of two iron atoms and two sulfur atoms into an iron-sulfur cluster.
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.

19 records

Show feature table

Start	End	DB	Term	Name
2	384	PIRSF	PIRSF005572	NifS
2	384	InterPro	IPR016454	Cysteine desulfurase
5	368	Pfam	PF00266	Aminotransferase class-V
5	368	InterPro	IPR000192	Aminotransferase class V domain
3	384	PANTHER	PTHR11601	CYSTEINE DESULFURYLASE FAMILY MEMBER
257	368	FunFam	G3DSA:3.90.1150.10:FF:000002	Cysteine desulfurase IscS
5	391	SUPERFAMILY	SSF53383	PLP-dependent transferases
5	391	InterPro	IPR015424	Pyridoxal phosphate-dependent transferase
16	263	FunFam	G3DSA:3.40.640.10:FF:000003	Cysteine desulfurase IscS
1	404	NCBIfam	TIGR02006	IscS subfamily cysteine desulfurase
1	404	InterPro	IPR010240	Cysteine desulfurase IscS
197	216	ProSitePatterns	PS00595	Aminotransferases class-V pyridoxal-phosphate attachment site.
197	216	InterPro	IPR020578	Aminotransferase class-V, pyridoxal-phosphate binding site
5	368	Gene3D	G3DSA:3.90.1150.10	Aspartate Aminotransferase, domain 1
5	368	InterPro	IPR015422	Pyridoxal phosphate-dependent transferase, small domain
16	263	Gene3D	G3DSA:3.40.640.10	-
16	263	InterPro	IPR015421	Pyridoxal phosphate-dependent transferase, major domain
1	395	Hamap	MF_00331	Cysteine desulfurase IscS [iscS].
1	395	InterPro	IPR010240	Cysteine desulfurase IscS

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 PA3814	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				0.506
5				0.396

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.

61 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
7TS	7CET	O25008	331.2 Da LogP 0.60 TPSA 157.9	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CNC2=CONC2=O)O`
8Q1	5USR	Q9Y697	540.7 Da LogP 3.29 TPSA 162.3	1 viol.	✓ Clean	`CCCCCCCCCCCC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)…`
C6P	5ZSS	A0A1I5NEH3	352.3 Da LogP 0.18 TPSA 149.2	1 viol.	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CN[C@@H](CS)C(=O)O)O`
DTT	6UXE	Q9Y697	154.3 Da LogP -0.43 TPSA 40.5	✓ Ro5	✓ Clean	`C([C@@H]([C@H](CS)O)O)S`
EDT	6UXE	Q9Y697	292.2 Da LogP -2.07 TPSA 155.7	✓ Ro5	✓ Clean	`C(CN(CC(=O)O)CC(=O)O)N(CC(=O)O)CC(=O)O`
ETE	6WI2	Q9Y697	208.3 Da LogP -0.33 TPSA 57.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCO`
FES	4EB5	O29689	175.8 Da LogP 1.29 TPSA 0.0	✓ Ro5	✓ Clean	`S1[Fe]S[Fe]1`
HCS	5WT5	O25008	135.2 Da LogP -0.28 TPSA 63.3	✓ Ro5	✓ Clean	`C(CS)[C@@H](C(=O)O)N`
P15	6UXE	Q9Y697	296.4 Da LogP -0.29 TPSA 75.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCO`
PDA	5WT6	O25008	320.2 Da LogP 0.27 TPSA 149.2	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CNC(C)C(=O)O)O`
PMP	4HVK	O29689	248.2 Da LogP 0.16 TPSA 125.9	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CN)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
ZINC1580161	1.000	208.3 Da LogP -0.33 TPSA 57.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCO`
ZINC16052118	1.000	340.4 Da LogP -0.28 TPSA 84.8	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCO`
ZINC16052257	1.000	384.5 Da LogP -0.26 TPSA 94.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC19364242	1.000	292.2 Da LogP -2.07 TPSA 155.7	✓ Ro5	✓ Clean	`O=C(O)CN(CCN(CC(=O)O)CC(=O)O)CC(=O)O`
ZINC34317654	1.000	472.6 Da LogP -0.23 TPSA 112.5	1 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC44076059	1.000	428.5 Da LogP -0.24 TPSA 103.3	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC5210101	1.000	252.3 Da LogP -0.31 TPSA 66.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCO`
ZINC5997860	1.000	296.4 Da LogP -0.29 TPSA 75.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCO`
ZINC19419017	0.933	393.3 Da LogP -2.68 TPSA 196.2	✓ Ro5	✓ Clean	`O=C(O)CN(CCN(CC(=O)O)CC(=O)O)CCN(CC(=O)O)CC(=O)O`
ZINC22593216	0.933	494.5 Da LogP -3.30 TPSA 236.8	1 viol.	✓ Clean	`O=C(O)CN(CCN(CCN(CC(=O)O)CC(=O)O)CC(=O)O)CCN(CC…`
ZINC1769289	0.765	306.3 Da LogP -1.68 TPSA 155.7	✓ Ro5	✓ Clean	`O=C(O)CN(CCCN(CC(=O)O)CC(=O)O)CC(=O)O`
ZINC4683946	0.765	320.3 Da LogP -1.29 TPSA 155.7	✓ Ro5	✓ Clean	`O=C(O)CN(CCCCN(CC(=O)O)CC(=O)O)CC(=O)O`
ZINC19364891	0.737	204.2 Da LogP -0.98 TPSA 81.1	✓ Ro5	✓ Clean	`CN(C)CCN(CC(=O)O)CC(=O)O`
ZINC19364892	0.737	232.3 Da LogP -0.20 TPSA 81.1	✓ Ro5	✓ Clean	`CCN(CC)CCN(CC(=O)O)CC(=O)O`
ZINC19366122	0.737	278.3 Da LogP -2.16 TPSA 138.6	✓ Ro5	✓ Clean	`O=C(O)CN(CCO)CCN(CC(=O)O)CC(=O)O`
ZINC33806192	0.737	320.3 Da LogP -1.29 TPSA 155.7	✓ Ro5	✓ Clean	`O=C(O)CCN(CCC(=O)O)CCN(CC(=O)O)CC(=O)O`
ZINC5908834	0.737	379.3 Da LogP -2.09 TPSA 196.2	✓ Ro5	✓ Clean	`O=C(O)CN(CCN(CCN(CC(=O)O)CC(=O)O)C(=O)O)CC(=O)O`
ZINC575419714	0.727	312.4 Da LogP 0.42 TPSA 66.4	✓ Ro5	✓ Clean	`COCCOCCOCCSCCOCCOCCO`
ZINC2527900	0.722	205.2 Da LogP -1.07 TPSA 115.1	✓ Ro5	✓ Clean	`O=C(O)CCN(CC(=O)O)CC(=O)O`
ZINC4261886	0.722	348.4 Da LogP -0.51 TPSA 155.7	✓ Ro5	✓ Clean	`O=C(O)CN(CCCCCCN(CC(=O)O)CC(=O)O)CC(=O)O`
ZINC115163232	0.700	222.3 Da LogP 0.07 TPSA 57.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCCO`
ZINC149813449	0.700	278.2 Da LogP -1.48 TPSA 155.7	✓ Ro5	✓ Clean	`O=C(O)CN(CCN(CC(=O)O)C(=O)O)CC(=O)O`
ZINC258837490	0.700	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCCO`
ZINC12501520	0.688	458.5 Da LogP -0.88 TPSA 123.5	1 viol.	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC1692489	0.688	222.3 Da LogP 0.33 TPSA 46.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOC`
ZINC3874716	0.688	414.5 Da LogP -0.90 TPSA 114.3	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC4283769	0.688	238.3 Da LogP -0.96 TPSA 77.4	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCO`
ZINC4521548	0.688	282.3 Da LogP -0.95 TPSA 86.6	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCO`
ZINC4530388	0.688	266.3 Da LogP 0.35 TPSA 55.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOC`
ZINC5178829	0.688	326.4 Da LogP -0.93 TPSA 95.8	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCO`
ZINC5178830	0.688	370.4 Da LogP -0.91 TPSA 105.1	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC5701172	0.688	310.4 Da LogP 0.36 TPSA 64.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOC`
ZINC5997861	0.688	398.5 Da LogP 0.40 TPSA 83.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOC`
ZINC22576460	0.684	320.3 Da LogP -1.29 TPSA 155.7	✓ Ro5	✓ Clean	`O=C(O)CCN(CCN(CCC(=O)O)CC(=O)O)CC(=O)O`
ZINC575432150	0.667	344.4 Da LogP -0.89 TPSA 100.5	✓ Ro5	✓ Clean	`COCCOCCOCCS(=O)(=O)CCOCCOCCO`
ZINC90669676	0.667	377.4 Da LogP -2.57 TPSA 176.0	✓ Ro5	✓ Clean	`O=CCN(CCN(CC(=O)O)CC(=O)O)CCN(CC(=O)O)CC(=O)O`
ZINC1532705	0.660	249.2 Da LogP 0.20 TPSA 120.1	✓ Ro5	✓ Clean	`Cc1ncc(COP(=O)(O)O)c(CO)c1O`
ZINC1857524240	0.652	207.3 Da LogP -0.75 TPSA 60.0	✓ Ro5	✓ Clean	`COCCNCCOCCOCCO`
ZINC22052182	0.650	336.3 Da LogP -2.05 TPSA 164.9	✓ Ro5	✓ Clean	`O=C(O)CN(CCOCCN(CC(=O)O)CC(=O)O)CC(=O)O`
ZINC217755395	0.636	263.2 Da LogP -1.47 TPSA 147.8	✓ Ro5	✓ Clean	`O=NN(CCN(CC(=O)O)CC(=O)O)CC(=O)O`
ZINC1532708	0.620	248.2 Da LogP 0.16 TPSA 125.9	✓ Ro5	✓ Clean	`Cc1ncc(COP(=O)(O)O)c(CN)c1O`
ZINC3055005	0.619	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCC[C@H](N)C(=O)O)C(=O)O`
ZINC3055007	0.619	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC3055010	0.619	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC3861663	0.619	380.4 Da LogP -2.04 TPSA 174.1	✓ Ro5	✓ Clean	`O=C(O)CN(CCOCCOCCN(CC(=O)O)CC(=O)O)CC(=O)O`
ZINC21297783	0.609	419.4 Da LogP -3.36 TPSA 179.8	✓ Ro5	✓ Clean	`CNC(=O)CN(CCN(CCN(CC(=O)O)CC(=O)NC)CC(=O)O)CC(=…`
ZINC5650743	0.600	222.3 Da LogP 0.07 TPSA 57.2	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCO`
ZINC6403917	0.600	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOCCOCCOCCO`
ZINC1555367	0.591	232.3 Da LogP 0.15 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC1720127	0.591	218.3 Da LogP -0.24 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCC[C@H](N)C(=O)O)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.