Protein profile

KP13_03674

ATP-dependent protease La

Genome: KpKP13

Gene: lon AHE46014.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GJ60
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Amino acids 784
Annotations 11
Features 52
PDB binders 6
Druggability 0.758

Overview

Basic information about this protein and its source genome.

Accession
KP13_03674
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
lon AHE46014.1
Status
annotated
Amino acids
784
Structure source
AlphaFold + ColabFold
EC
3.4.21.53
GO
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: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: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: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
hit
Human identity (%)
54.762
Human E-value
9.05e-63
Gut microbiome off-target
hit
Essential (DEG)
Y
DEG identity (%)
98.98
DEG E-value
0.0
Localization
Cytoplasmic
ColabFold pLDDT
88.68

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 0.758
Structure A0A0H3GJ60
Pocket Pocket 7
P2Rank 0.783
Structure A0A0H3GJ60
Pocket Pocket 1
ColabFold model
FPocket 0.438 · Pocket 5
P2Rank 0.77 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 556 / 4744 genomes with a hit
Normalized 0.117

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 10 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

10
  • 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: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: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:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
  • GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • 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.

Sequence Features

Domain/signature hits from InterPro and related databases.

52 records
Show feature table
Start End DB Term Name
313 490 Gene3D G3DSA:3.40.50.300 -
313 490 InterPro IPR027417 P-loop containing nucleoside triphosphate hydrolase
1 775 PIRSF PIRSF001174 Lon_proteas
1 775 InterPro IPR004815 Lon protease, bacterial/eukaryotic-type
348 492 SMART SM00382 AAA_5
348 492 InterPro IPR003593 AAA+ ATPase domain
120 245 FunFam G3DSA:1.20.58.1480:FF:000001 Lon protease
313 493 CDD cd19500 RecA-like_Lon
356 375 PRINTS PR00830 Endopeptidase La (Lon) serine protease (S16) signature
726 744 PRINTS PR00830 Endopeptidase La (Lon) serine protease (S16) signature
595 611 PRINTS PR00830 Endopeptidase La (Lon) serine protease (S16) signature
673 692 PRINTS PR00830 Endopeptidase La (Lon) serine protease (S16) signature
703 722 PRINTS PR00830 Endopeptidase La (Lon) serine protease (S16) signature
12 778 PANTHER PTHR10046 ATP DEPENDENT LON PROTEASE FAMILY MEMBER
12 778 InterPro IPR027065 Lon protease
1 118 FunFam G3DSA:2.30.130.40:FF:000001 Lon protease
190 227 Coils Coil Coil
595 771 SUPERFAMILY SSF54211 Ribosomal protein S5 domain 2-like
595 771 InterPro IPR020568 Ribosomal protein S5 domain 2-type fold
11 772 Hamap MF_01973 Lon protease [lon].
11 772 InterPro IPR027543 Lon protease, bacterial
592 773 ProSiteProfiles PS51786 Lon proteolytic domain profile.
592 773 InterPro IPR008269 Peptidase S16, Lon proteolytic domain
676 684 ProSitePatterns PS01046 ATP-dependent serine proteases, lon family, serine active site.
676 684 InterPro IPR008268 Peptidase S16, active site
352 489 Pfam PF00004 ATPase family associated with various cellular activities (AAA)
352 489 InterPro IPR003959 ATPase, AAA-type, core
12 771 NCBIfam TIGR00763 endopeptidase La
12 771 InterPro IPR004815 Lon protease, bacterial/eukaryotic-type
313 490 FunFam G3DSA:3.40.50.300:FF:000021 Lon protease homolog
120 245 Gene3D G3DSA:1.20.58.1480 -
491 584 Gene3D G3DSA:1.10.8.60 -
10 202 SMART SM00464 lon_5
10 202 InterPro IPR003111 Lon protease, N-terminal domain
585 772 FunFam G3DSA:3.30.230.10:FF:000010 Lon protease
10 201 Pfam PF02190 ATP-dependent protease La (LON) substrate-binding domain
10 201 InterPro IPR003111 Lon protease, N-terminal domain
585 772 Gene3D G3DSA:3.30.230.10 -
585 772 InterPro IPR014721 Ribosomal protein S5 domain 2-type fold, subgroup
491 584 FunFam G3DSA:1.10.8.60:FF:000035 Lon protease
570 772 Pfam PF05362 Lon protease (S16) C-terminal proteolytic domain
570 772 InterPro IPR008269 Peptidase S16, Lon proteolytic domain
313 587 SUPERFAMILY SSF52540 P-loop containing nucleoside triphosphate hydrolases
313 587 InterPro IPR027417 P-loop containing nucleoside triphosphate hydrolase
11 202 ProSiteProfiles PS51787 Lon N-terminal domain profile.
11 202 InterPro IPR003111 Lon protease, N-terminal domain
253 300 Gene3D G3DSA:1.20.5.5270 -
252 301 FunFam G3DSA:1.20.5.5270:FF:000002 Lon protease homolog
1 118 Gene3D G3DSA:2.30.130.40 -
1 118 InterPro IPR046336 Lon protease, N-terminal domain superfamily
10 201 SUPERFAMILY SSF88697 PUA domain-like
10 201 InterPro IPR015947 PUA-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.

3D visualization script Full viewer

Loading 3D structure...

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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_A0A0H3GJ60
AlphaFold — — full sequence — Viewing
ColabFold KP13_03674
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
7 0.758
44 0.29

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 Sticks Spheres Surfaces Score Probability Labels Zoom Positions
1 10.49 0.564
2 2.22 0.054
3 1.41 0.018

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.