Protein profile

KP13_03869

putative protease La

Genome: KpKP13

Gene: AHE45384.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GR39
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Amino acids 585
Annotations 6
Features 17
PDB binders 5
Druggability 0.16

Overview

Basic information about this protein and its source genome.

Accession
KP13_03869
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
AHE45384.1
Status
annotated
Amino acids
585
Structure source
AlphaFold + ColabFold
EC
3.4.21.53
GO
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: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.

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
Human identity (%)
0.0
Gut microbiome off-target
hit
Essential (DEG)
Y
DEG identity (%)
44.182
DEG E-value
8.85e-145
Localization
Cytoplasmic
ColabFold pLDDT
93.22

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 0.16
Structure A0A0H3GR39
Pocket Pocket 26
P2Rank 0.485
Structure A0A0H3GR39
Pocket Pocket 1
ColabFold model
FPocket 0.201 · Pocket 30
P2Rank 0.607 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 93 / 4744 genomes with a hit
Normalized 0.02

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)

1

Gene Ontology (GO)

5
  • 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: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.

Sequence Features

Domain/signature hits from InterPro and related databases.

17 records
Show feature table
Start End DB Term Name
492 510 PRINTS PR00830 Endopeptidase La (Lon) serine protease (S16) signature
432 451 PRINTS PR00830 Endopeptidase La (Lon) serine protease (S16) signature
462 481 PRINTS PR00830 Endopeptidase La (Lon) serine protease (S16) signature
435 521 Pfam PF05362 Lon protease (S16) C-terminal proteolytic domain
435 521 InterPro IPR008269 Peptidase S16, Lon proteolytic domain
349 540 SUPERFAMILY SSF54211 Ribosomal protein S5 domain 2-like
349 540 InterPro IPR020568 Ribosomal protein S5 domain 2-type fold
58 228 Gene3D G3DSA:3.40.50.300 -
58 228 InterPro IPR027417 P-loop containing nucleoside triphosphate hydrolase
346 543 ProSiteProfiles PS51786 Lon proteolytic domain profile.
346 543 InterPro IPR008269 Peptidase S16, Lon proteolytic domain
114 224 Pfam PF13654 LonB-like, AAA domain
114 224 InterPro IPR041699 Lon protease, AAA domain
321 551 PANTHER PTHR10046 ATP DEPENDENT LON PROTEASE FAMILY MEMBER
321 551 InterPro IPR027065 Lon protease
326 567 Gene3D G3DSA:3.30.230.10 -
326 567 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.

3D visualization script Full viewer

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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_A0A0H3GR39
AlphaFold — — full sequence — Viewing
ColabFold KP13_03869
ColabFold — — full sequence — Loaded
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

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 5.22 0.243
2 4.52 0.193
3 1.73 0.031
4 1.59 0.025
5 1.38 0.017

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

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
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

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.