Protein profile

PA4576

ATP-dependent protease

Genome: NC_002516.2

Gene: PA4576 Structure source: AlphaFold UniProt Q9HVK8

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Amino acids 817

Annotations 6

Features 29

PDB binders 5

Druggability 0.939

Overview

Basic information about this protein and its source genome.

Accession: PA4576
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA4576
Status: annotated
Amino acids: 817
Structure source: AlphaFold

3.4.21.53

GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0004176 Catalysis of the hydrolysis of peptide bonds, driven by ATP hydrolysis. GO:0004252 Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine). GO:0030163 The chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds. GO:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Gut microbiome off-target: hit
Essential (DEG): N
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 0.939

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

Enzyme Commission (EC)

3.4.21.53

Gene Ontology (GO)

GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0004176 Catalysis of the hydrolysis of peptide bonds, driven by ATP hydrolysis.
GO:0004252 Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
GO:0030163 The chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds.
GO:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.

Sequence Features

Domain/signature hits from InterPro and related databases.

29 records

Show feature table

Start	End	DB	Term	Name
451	537	Gene3D	G3DSA:1.10.8.60	-
35	536	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
35	536	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
650	754	Pfam	PF05362	Lon protease (S16) C-terminal proteolytic domain
650	754	InterPro	IPR008269	Peptidase S16, Lon proteolytic domain
677	696	PRINTS	PR00830	Endopeptidase La (Lon) serine protease (S16) signature
566	582	PRINTS	PR00830	Endopeptidase La (Lon) serine protease (S16) signature
647	666	PRINTS	PR00830	Endopeptidase La (Lon) serine protease (S16) signature
707	725	PRINTS	PR00830	Endopeptidase La (Lon) serine protease (S16) signature
66	85	PRINTS	PR00830	Endopeptidase La (Lon) serine protease (S16) signature
476	540	Pfam	PF20436	Archaeal LonB, AAA+ ATPase LID domain
476	540	InterPro	IPR046843	LonB, AAA+ ATPase LID domain, archaeal-type
122	762	PANTHER	PTHR10046	ATP DEPENDENT LON PROTEASE FAMILY MEMBER
122	762	InterPro	IPR027065	Lon protease
92	125	Pfam	PF20437	Lon-like LonC helical domain
92	125	InterPro	IPR046844	Lon-like, helical domain
563	758	ProSiteProfiles	PS51786	Lon proteolytic domain profile.
563	758	InterPro	IPR008269	Peptidase S16, Lon proteolytic domain
317	448	Pfam	PF13654	LonB-like, AAA domain
317	448	InterPro	IPR041699	Lon protease, AAA domain
9	187	Gene3D	G3DSA:3.40.50.300	-
9	187	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
188	450	Gene3D	G3DSA:3.40.50.300	-
188	450	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
789	817	MobiDBLite	mobidb-lite	consensus disorder prediction
565	757	SUPERFAMILY	SSF54211	Ribosomal protein S5 domain 2-like
565	757	InterPro	IPR020568	Ribosomal protein S5 domain 2-type fold
543	775	Gene3D	G3DSA:3.30.230.10	-
543	775	InterPro	IPR014721	Ribosomal protein S5 domain 2-type fold, subgroup

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 PA4576	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
11				0.939
9				0.652
4				0.303
2				0.211

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
BO2	4FWD	C9DRU9	384.2 Da LogP 0.36 TPSA 124.4	✓ Ro5	✓ Clean	`B([C@H](CC(C)C)NC(=O)[C@H](Cc1ccccc1)NC(=O)c2cn…`
CIX	4FWH	C9DRU9	491.4 Da LogP 2.40 TPSA 137.0	✓ Ro5	✓ Clean	`B([C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C…`
PE4	3K1J	B6YU74	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOCCOCCOCCO`
PE8	3K1J	B6YU74	370.4 Da LogP -0.91 TPSA 105.1	✓ Ro5	✓ Clean	`C(COCCOCCOCCOCCOCCOCCOCCO)O`
SLA	4FWG	C9DRU9	215.2 Da LogP -0.93 TPSA 86.6	✓ Ro5	✓ Clean	`C[C@@H]1[C@@H]([C@@](NC1=O)(C=O)[C@H](C(C)C)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
ZINC12501520	1.000	458.5 Da LogP -0.88 TPSA 123.5	1 viol.	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC200269110	1.000	491.4 Da LogP 2.40 TPSA 137.0	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)OCc1ccccc1)C(=O)N[C@H](CC(C)C…`
ZINC3874716	1.000	414.5 Da LogP -0.90 TPSA 114.3	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC4283769	1.000	238.3 Da LogP -0.96 TPSA 77.4	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCO`
ZINC4521548	1.000	282.3 Da LogP -0.95 TPSA 86.6	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCO`
ZINC5178829	1.000	326.4 Da LogP -0.93 TPSA 95.8	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCO`
ZINC5178830	1.000	370.4 Da LogP -0.91 TPSA 105.1	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC5650743	1.000	222.3 Da LogP 0.07 TPSA 57.2	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCO`
ZINC6403917	1.000	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOCCOCCOCCO`
ZINC95093215	0.843	356.4 Da LogP 1.30 TPSA 104.2	✓ Ro5	✓ Clean	`CC(C)C[C@@H](O)NC(=O)[C@H](Cc1ccccc1)NC(=O)c1cn…`
ZINC95093216	0.843	356.4 Da LogP 1.30 TPSA 104.2	✓ Ro5	✓ Clean	`CC(C)C[C@H](O)NC(=O)[C@H](Cc1ccccc1)NC(=O)c1cnc…`
ZINC19892130	0.773	468.6 Da LogP 4.60 TPSA 93.7	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)[C@@H](CC(C)C)NC(=O)OCc1ccccc…`
ZINC19892133	0.773	468.6 Da LogP 4.60 TPSA 93.7	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)OCc1ccccc1)C(=O)N[C@@H](CC(C)…`
ZINC19892137	0.773	468.6 Da LogP 4.60 TPSA 93.7	✓ Ro5	✓ Clean	`CC(C)C[C@@H](NC(=O)OCc1ccccc1)C(=O)N[C@H](CC(C)…`
ZINC19892139	0.773	468.6 Da LogP 4.60 TPSA 93.7	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)OCc1ccccc1)C(=O)N[C@H](CC(C)C…`
ZINC4598914	0.773	378.5 Da LogP 2.94 TPSA 104.7	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1…`
ZINC4598915	0.773	378.5 Da LogP 2.94 TPSA 104.7	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)[C@@H](CC(C)C)NC(=O)OCc1ccccc…`
ZINC4598916	0.773	378.5 Da LogP 2.94 TPSA 104.7	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)OCc1ccccc1)C(=O)N[C@H](CC(C)C…`
ZINC4598917	0.773	378.5 Da LogP 2.94 TPSA 104.7	✓ Ro5	✓ Clean	`CC(C)C[C@@H](NC(=O)[C@@H](CC(C)C)NC(=O)OCc1cccc…`
ZINC4458753	0.756	392.5 Da LogP 3.03 TPSA 93.7	✓ Ro5	✓ Clean	`COC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OC…`
ZINC4458754	0.756	392.5 Da LogP 3.03 TPSA 93.7	✓ Ro5	✓ Clean	`COC(=O)[C@H](CC(C)C)NC(=O)[C@@H](CC(C)C)NC(=O)O…`
ZINC4458761	0.756	392.5 Da LogP 3.03 TPSA 93.7	✓ Ro5	✓ Clean	`COC(=O)[C@@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)O…`
ZINC4458763	0.756	392.5 Da LogP 3.03 TPSA 93.7	✓ Ro5	✓ Clean	`COC(=O)[C@@H](CC(C)C)NC(=O)[C@@H](CC(C)C)NC(=O)…`
ZINC4764236	0.756	377.5 Da LogP 2.34 TPSA 110.5	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)[C@@H](CC(C)C)NC(=O)OCc1ccccc…`
ZINC4764244	0.756	377.5 Da LogP 2.34 TPSA 110.5	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1…`
ZINC4764718	0.756	426.5 Da LogP 3.58 TPSA 93.7	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)OCc1ccccc1)C(=O)N[C@@H](C)C(=…`
ZINC4764725	0.756	426.5 Da LogP 3.58 TPSA 93.7	✓ Ro5	✓ Clean	`CC(C)C[C@@H](NC(=O)OCc1ccccc1)C(=O)N[C@@H](C)C(…`
ZINC1875255061	0.745	405.5 Da LogP 2.95 TPSA 87.7	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)[C@@H](CC(C)C)NC(=O)OCc1ccccc…`
ZINC1875255062	0.745	405.5 Da LogP 2.95 TPSA 87.7	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)OCc1ccccc1)C(=O)N[C@@H](CC(C)…`
ZINC1875255063	0.745	405.5 Da LogP 2.95 TPSA 87.7	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)OCc1ccccc1)C(=O)N[C@H](CC(C)C…`
ZINC1875255064	0.745	405.5 Da LogP 2.95 TPSA 87.7	✓ Ro5	✓ Clean	`CC(C)C[C@@H](NC(=O)OCc1ccccc1)C(=O)N[C@H](CC(C)…`
ZINC141072414	0.723	350.4 Da LogP 2.31 TPSA 104.7	✓ Ro5	✓ Clean	`CC[C@H](NC(=O)[C@@H](CC(C)C)NC(=O)OCc1ccccc1)C(…`
ZINC2562540	0.723	350.4 Da LogP 2.31 TPSA 104.7	✓ Ro5	✓ Clean	`CC[C@H](NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1)C(=…`
ZINC4899622	0.723	412.5 Da LogP 3.14 TPSA 104.7	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)OCc1ccccc1)C(=O)N[C@@H](Cc1cc…`
ZINC1576107	0.717	336.4 Da LogP 1.92 TPSA 104.7	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)OCc1ccccc1)C(=O)N[C@@H](C)C(=…`
ZINC1576108	0.717	336.4 Da LogP 1.92 TPSA 104.7	✓ Ro5	✓ Clean	`CC(C)C[C@@H](NC(=O)OCc1ccccc1)C(=O)N[C@@H](C)C(…`
ZINC1576109	0.717	336.4 Da LogP 1.92 TPSA 104.7	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)OCc1ccccc1)C(=O)N[C@H](C)C(=O…`
ZINC1576110	0.717	336.4 Da LogP 1.92 TPSA 104.7	✓ Ro5	✓ Clean	`CC(C)C[C@@H](NC(=O)OCc1ccccc1)C(=O)N[C@H](C)C(=…`
ZINC34405577	0.711	278.4 Da LogP 2.07 TPSA 67.4	✓ Ro5	✓ Clean	`CNC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1`
ZINC34405578	0.711	278.4 Da LogP 2.07 TPSA 67.4	✓ Ro5	✓ Clean	`CNC(=O)[C@@H](CC(C)C)NC(=O)OCc1ccccc1`
ZINC4535614	0.708	412.5 Da LogP 3.14 TPSA 104.7	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)[C@@H](Cc1ccccc1)NC(=O)OCc1cc…`
ZINC4535619	0.708	412.5 Da LogP 3.14 TPSA 104.7	✓ Ro5	✓ Clean	`CC(C)C[C@@H](NC(=O)[C@@H](Cc1ccccc1)NC(=O)OCc1c…`
ZINC4535621	0.708	412.5 Da LogP 3.14 TPSA 104.7	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)[C@H](Cc1ccccc1)NC(=O)OCc1ccc…`
ZINC4535624	0.708	412.5 Da LogP 3.14 TPSA 104.7	✓ Ro5	✓ Clean	`CC(C)C[C@@H](NC(=O)[C@H](Cc1ccccc1)NC(=O)OCc1cc…`
ZINC4760653	0.708	351.4 Da LogP 0.29 TPSA 130.8	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)OCc1ccccc1)C(=O)N[C@@H](CO)C(…`
ZINC4899829	0.708	411.5 Da LogP 2.54 TPSA 110.5	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)OCc1ccccc1)C(=O)N[C@@H](Cc1cc…`
ZINC5028479	0.708	479.6 Da LogP 1.51 TPSA 143.1	✓ Ro5	✓ Clean	`COC(=O)[C@H](CO)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H]…`
ZINC5028481	0.708	479.6 Da LogP 1.51 TPSA 143.1	✓ Ro5	✓ Clean	`COC(=O)[C@H](CO)NC(=O)[C@@H](CC(C)C)NC(=O)[C@@H…`
ZINC5028482	0.708	479.6 Da LogP 1.51 TPSA 143.1	✓ Ro5	✓ Clean	`COC(=O)[C@@H](CO)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H…`
ZINC5028484	0.708	479.6 Da LogP 1.51 TPSA 143.1	✓ Ro5	✓ Clean	`COC(=O)[C@@H](CO)NC(=O)[C@@H](CC(C)C)NC(=O)[C@@…`

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.