Protein profile

PA0779

ATP-dependent protease

Genome: NC_002516.2

Gene: PA0779 lon Structure source: AlphaFold UniProt Q9I5F9
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Amino acids 799
Annotations 13
Features 49
PDB binders 6
Druggability 0.799

Overview

Basic information about this protein and its source genome.

Accession
PA0779
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA0779 lon
Status
annotated
Amino acids
799
Structure source
AlphaFold
EC
3.4.21.53
GO
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0016887 Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient. GO:0004176 Catalysis of the hydrolysis of peptide bonds, driven by ATP hydrolysis. GO:0043565 Binding to DNA of a specific nucleotide composition, e.g. GC-rich DNA binding, or with a specific sequence motif or type of DNA e.g. promotor binding or rDNA binding. 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).

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
52.239
Human E-value
1.28e-13
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 0.799
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 12 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

12
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
  • GO:0016887 Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
  • GO:0004176 Catalysis of the hydrolysis of peptide bonds, driven by ATP hydrolysis.
  • GO:0043565 Binding to DNA of a specific nucleotide composition, e.g. GC-rich DNA binding, or with a specific sequence motif or type of DNA e.g. promotor binding or rDNA binding.
  • 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:0071236 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an antibiotic stimulus. An antibiotic is a chemical substance produced by a microorganism which has the capacity to inhibit the growth of or to kill other microorganisms.
  • GO:0034605 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a heat stimulus, a temperature stimulus above the optimal temperature for that organism.
  • GO:0006515 The chemical reactions and pathways resulting in the breakdown of misfolded or attenuated proteins.
  • GO:0080164 Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving nitric oxide, nitrogen monoxide (NO), a colorless gas only slightly soluble in water.
  • 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.

49 records
Show feature table
Start End DB Term Name
225 245 Coils Coil Coil
25 139 Gene3D G3DSA:2.30.130.40 -
25 139 InterPro IPR046336 Lon protease, N-terminal domain superfamily
279 328 FunFam G3DSA:1.20.5.5270:FF:000002 Lon protease homolog
32 228 ProSiteProfiles PS51787 Lon N-terminal domain profile.
32 228 InterPro IPR003111 Lon protease, N-terminal domain
146 270 Gene3D G3DSA:1.20.58.1480 -
620 797 SUPERFAMILY SSF54211 Ribosomal protein S5 domain 2-like
620 797 InterPro IPR020568 Ribosomal protein S5 domain 2-type fold
21 799 PIRSF PIRSF001174 Lon_proteas
21 799 InterPro IPR004815 Lon protease, bacterial/eukaryotic-type
379 517 Pfam PF00004 ATPase family associated with various cellular activities (AAA)
379 517 InterPro IPR003959 ATPase, AAA-type, core
375 520 SMART SM00382 AAA_5
375 520 InterPro IPR003593 AAA+ ATPase domain
32 798 Hamap MF_01973 Lon protease [lon].
32 798 InterPro IPR027543 Lon protease, bacterial
617 799 ProSiteProfiles PS51786 Lon proteolytic domain profile.
617 799 InterPro IPR008269 Peptidase S16, Lon proteolytic domain
340 518 Gene3D G3DSA:3.40.50.300 -
340 518 InterPro IPR027417 P-loop containing nucleoside triphosphate hydrolase
340 521 CDD cd19500 RecA-like_Lon
519 611 Gene3D G3DSA:1.10.8.60 -
32 227 Pfam PF02190 ATP-dependent protease La (LON) substrate-binding domain
32 227 InterPro IPR003111 Lon protease, N-terminal domain
337 614 SUPERFAMILY SSF52540 P-loop containing nucleoside triphosphate hydrolases
337 614 InterPro IPR027417 P-loop containing nucleoside triphosphate hydrolase
32 227 SUPERFAMILY SSF88697 PUA domain-like
32 227 InterPro IPR015947 PUA-like superfamily
615 799 Gene3D G3DSA:3.30.230.10 -
615 799 InterPro IPR014721 Ribosomal protein S5 domain 2-type fold, subgroup
146 270 FunFam G3DSA:1.20.58.1480:FF:000008 Lon protease
597 797 Pfam PF05362 Lon protease (S16) C-terminal proteolytic domain
597 797 InterPro IPR008269 Peptidase S16, Lon proteolytic domain
702 710 ProSitePatterns PS01046 ATP-dependent serine proteases, lon family, serine active site.
702 710 InterPro IPR008268 Peptidase S16, active site
729 748 PRINTS PR00830 Endopeptidase La (Lon) serine protease (S16) signature
620 636 PRINTS PR00830 Endopeptidase La (Lon) serine protease (S16) signature
383 402 PRINTS PR00830 Endopeptidase La (Lon) serine protease (S16) signature
752 770 PRINTS PR00830 Endopeptidase La (Lon) serine protease (S16) signature
699 718 PRINTS PR00830 Endopeptidase La (Lon) serine protease (S16) signature
279 328 Gene3D G3DSA:1.20.5.5270 -
34 797 NCBIfam TIGR00763 endopeptidase La
34 797 InterPro IPR004815 Lon protease, bacterial/eukaryotic-type
340 518 FunFam G3DSA:3.40.50.300:FF:000021 Lon protease homolog
31 228 SMART SM00464 lon_5
31 228 InterPro IPR003111 Lon protease, N-terminal domain
31 594 PANTHER PTHR43718 LON PROTEASE
31 594 InterPro IPR027065 Lon protease

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 PA0779
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
5 0.799
1 0.282

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.

74 records

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.

Show only:
Ligand Source crystal UniProt (homolog) MW · LogP · TPSA Lipinski PAINS SMILES
4KZ
4YPL
A0A059VAZ3 418.3 Da LogP 0.56 TPSA 124.4 ✓ Ro5 ✓ Clean B([C@H](Cc1ccccc1)NC(=O)[C@H](Cc2ccccc2)NC(=O)c…
AGS
6WQH
A0A059VAZ3 523.2 Da LogP -1.51 TPSA 262.1 3 viol. ✓ Clean c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…
BO2
6X27
P36776 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…
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
UFY
6WZV
P36776 384.2 Da LogP 0.36 TPSA 124.4 ✓ Ro5 ✓ Clean B([C@H](CC(C)C)NC(=O)[C@@H](Cc1ccccc1)NC(=O)c2c…

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.