Protein profile

PA3724

elastase LasB

Genome: NC_002516.2

Gene: lasB PA3724 Structure source: Experimental + AlphaFold UniProt P14756
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Amino acids 498
Annotations 10
Features 32
PDB binders 98
Druggability 0.554

Overview

Basic information about this protein and its source genome.

Accession
PA3724
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
lasB PA3724
Status
annotated
Amino acids
498
Structure source
Experimental + AlphaFold
EC
3.4.24.26
GO
GO:0005576 The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. GO:0004175 Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain. GO:0046872 Binding to a metal ion. GO:0004222 Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions. GO:0071978 Bacterial-type flagellum-dependent cell motility in which the action of numerous flagella results in the smooth movement of a group of cells along a solid surface. Swarming motility is observed in groups of bacteria. GO:0015628 The process in which proteins are secreted across the outer membrane of Gram-negative bacteria by the type II secretion system. Proteins using this pathway are first translocated across the cytoplasmic membrane via the Sec or Tat pathways.

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
Gut microbiome off-target
hit
Essential (DEG)
N
Localization
Extracellular

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 0.554
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

9
  • GO:0005576 The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.
  • GO:0004175 Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain.
  • GO:0046872 Binding to a metal ion.
  • GO:0004222 Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.
  • GO:0071978 Bacterial-type flagellum-dependent cell motility in which the action of numerous flagella results in the smooth movement of a group of cells along a solid surface. Swarming motility is observed in groups of bacteria.
  • GO:0015628 The process in which proteins are secreted across the outer membrane of Gram-negative bacteria by the type II secretion system. Proteins using this pathway are first translocated across the cytoplasmic membrane via the Sec or Tat pathways.
  • GO:0043952 The process in which unfolded proteins are transported across the cytoplasmic membrane in Gram-positive and Gram-negative bacteria by the Sec complex, in a process involving proteolytic cleavage of an N-terminal signal peptide.
  • GO:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
  • GO:0044010 A process in which planktonically growing microorganisms of the same species grow at a liquid-air interface or on a solid substrate under the flow of a liquid and produce extracellular polymers that facilitate matrix formation, resulting in a change in the organisms' growth rate and gene transcription.

Sequence Features

Domain/signature hits from InterPro and related databases.

32 records
Show feature table
Start End DB Term Name
419 435 PRINTS PR00730 Thermolysin metalloprotease (M4) family signature
419 435 InterPro IPR023612 Peptidase M4
336 352 PRINTS PR00730 Thermolysin metalloprotease (M4) family signature
336 352 InterPro IPR023612 Peptidase M4
357 368 PRINTS PR00730 Thermolysin metalloprotease (M4) family signature
357 368 InterPro IPR023612 Peptidase M4
302 322 PRINTS PR00730 Thermolysin metalloprotease (M4) family signature
302 322 InterPro IPR023612 Peptidase M4
198 349 FunFam G3DSA:3.10.170.10:FF:000002 Elastase
348 492 Pfam PF02868 Thermolysin metallopeptidase, alpha-helical domain
348 492 InterPro IPR001570 Peptidase M4, C-terminal
1 23 SignalP_GRAM_NEGATIVE SignalP-noTM SignalP-noTM
24 498 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
118 197 Gene3D G3DSA:3.10.450.40 -
34 492 PANTHER PTHR33794 BACILLOLYSIN
199 494 SUPERFAMILY SSF55486 Metalloproteases ("zincins"), catalytic domain
234 492 CDD cd09597 M4_TLP
123 192 Pfam PF03413 Peptidase propeptide and YPEB domain
123 192 InterPro IPR025711 PepSY domain
30 115 Gene3D G3DSA:3.10.450.490 -
1 3 Phobius SIGNAL_PEPTIDE_N_REGION N-terminal region of a signal peptide.
198 349 Gene3D G3DSA:3.10.170.10 -
208 345 Pfam PF01447 Thermolysin metallopeptidase, catalytic domain
208 345 InterPro IPR013856 Peptidase M4 domain
56 90 Pfam PF07504 Fungalysin/Thermolysin Propeptide Motif
56 90 InterPro IPR011096 FTP domain
1 23 Phobius SIGNAL_PEPTIDE Signal peptide region
16 23 Phobius SIGNAL_PEPTIDE_C_REGION C-terminal region of a signal peptide.
1 23 SignalP_GRAM_POSITIVE SignalP-TM SignalP-TM
350 497 Gene3D G3DSA:1.10.390.10 Neutral Protease Domain 2
350 497 InterPro IPR027268 Peptidase M4/M1, CTD superfamily
4 15 Phobius SIGNAL_PEPTIDE_H_REGION Hydrophobic region of a signal peptide.

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

18 + 1

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry Method Resolution Chain Coverage Links Status
PDB 8CR3
X-ray 1.12 Å A
95.4% 24-498
PDBe RCSB PDBj File
Viewing
PDB 8R1B
X-ray 1.31 Å A
95.4% 24-498
PDBe RCSB PDBj File
Loaded
PDB 8CR7
X-ray 1.50 Å A,B
95.4% 24-498
PDBe RCSB PDBj File
Loaded
PDB 6F8B
X-ray 1.30 Å A
60.4% 198-498
PDBe RCSB PDBj File
Loaded
PDB 1U4G
X-ray 1.40 Å A
60.4% 198-498
PDBe RCSB PDBj File
Loaded
PDB 3DBK
X-ray 1.40 Å A
60.4% 198-498
PDBe RCSB PDBj File
Loaded
PDB 1EZM
X-ray 1.50 Å A
60.4% 198-498
PDBe RCSB PDBj File
Loaded
PDB 7Z68
X-ray 1.50 Å A
60.4% 198-498
PDBe RCSB PDBj File
Loaded
PDB 7OC7
X-ray 1.95 Å A
60.4% 198-498
PDBe RCSB PDBj File
Loaded
PDB 6FZX
X-ray 2.10 Å A
60.4% 198-498
PDBe RCSB PDBj File
Loaded
PDB 8CC4
X-ray 2.70 Å A,B
60.4% 198-498
PDBe RCSB PDBj File
Loaded
PDB 7QH1
X-ray 2.74 Å A,B,C,D
60.4% 198-498
PDBe RCSB PDBj File
Loaded
PDB 9FS0
X-ray 1.30 Å A
60.4% 198-498
PDBe RCSB PDBj File
Metadata only
PDB 9FQE
X-ray 1.60 Å A
60.4% 198-498
PDBe RCSB PDBj File
Metadata only
PDB 9FQY
X-ray 1.60 Å A
60.4% 198-498
PDBe RCSB PDBj File
Metadata only
PDB 9FQD
X-ray 1.70 Å A
60.4% 198-498
PDBe RCSB PDBj File
Metadata only
PDB 9FRZ
X-ray 1.70 Å A
60.4% 198-498
PDBe RCSB PDBj File
Metadata only
PDB 9FQX
X-ray 1.80 Å A
60.4% 198-498
PDBe RCSB PDBj File
Metadata only
AlphaFold PA3724
AlphaFold — — 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
1 0.554

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 18.37 0.821
2 1.87 0.037
3 1.44 0.019

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.

235 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.

Show only:
Ligand Source crystal MW · LogP · TPSA Lipinski PAINS SMILES
CXH
6F8B 1.30 Å Open crystal
236.1 Da LogP 2.86 TPSA 29.1 ✓ Ro5 ✓ Clean c1cc(c(cc1NC(=O)CS)Cl)Cl
EEK
6FZX 2.10 Å Open crystal
263.1 Da LogP 1.83 TPSA 78.4 ✓ Ro5 ✓ Clean c1cc(c(cc1NC(=O)CC(=O)NO)Cl)Cl
HPI
1U4G 1.40 Å Open crystal
441.5 Da LogP 0.72 TPSA 158.8 ✓ Ro5 ✓ Clean c1ccc(cc1)CC[C@@H](C(=O)O)N[C@@H](Cc2ccccc2)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.