Protein profile

PA3764

membrane-bound lytic murein transglycosylase F

Genome: NC_002516.2

Gene: PA3764 mltF Structure source: Experimental + AlphaFold UniProt Q9HXN1
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Amino acids 452
Annotations 9
Features 20
PDB binders 3
Druggability 0.887

Overview

Basic information about this protein and its source genome.

Accession
PA3764
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA3764 mltF
Status
annotated
Amino acids
452
Structure source
Experimental + AlphaFold
EC
4.2.2.n1
GO
GO:0009279 A lipid bilayer that forms the outermost membrane of the cell envelope; enriched in polysaccharide and protein; the outer leaflet of the membrane contains specific lipopolysaccharide structures. GO:0008933 Catalysis of the cleavage of a peptidoglycan chain into a peptidoglycan chain with N-acetyl-1,6-anhydromuramyl-[peptide] at the reducing end + a peptidoglycan chain with N-acetylglucosamine at the non-reducing end. Includes endolytic transglycosylase activity that fragments the glycan chain internally and exolytic transgylcosylase activity that cleaves a terminal disaccharide from the end of the glycan strand. GO:0016998 The chemical reactions and pathways resulting in the breakdown of macromolecules that form part of a cell wall. GO:0071555 A process that results in the assembly, arrangement of constituent parts, or disassembly of the cell wall, the rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal and most prokaryotic cells, maintaining their shape and protecting them from osmotic lysis. GO:0009253 The chemical reactions and pathways resulting in the breakdown of peptidoglycans, any of a class of glycoconjugates found in bacterial cell walls and consisting of long glycan strands of alternating residues of beta-(1,4) linked N-acetylglucosamine and N-acetylmuramic acid, cross-linked by short peptides. GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.

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 0.887
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

8
  • GO:0009279 A lipid bilayer that forms the outermost membrane of the cell envelope; enriched in polysaccharide and protein; the outer leaflet of the membrane contains specific lipopolysaccharide structures.
  • GO:0008933 Catalysis of the cleavage of a peptidoglycan chain into a peptidoglycan chain with N-acetyl-1,6-anhydromuramyl-[peptide] at the reducing end + a peptidoglycan chain with N-acetylglucosamine at the non-reducing end. Includes endolytic transglycosylase activity that fragments the glycan chain internally and exolytic transgylcosylase activity that cleaves a terminal disaccharide from the end of the glycan strand.
  • GO:0016998 The chemical reactions and pathways resulting in the breakdown of macromolecules that form part of a cell wall.
  • GO:0071555 A process that results in the assembly, arrangement of constituent parts, or disassembly of the cell wall, the rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal and most prokaryotic cells, maintaining their shape and protecting them from osmotic lysis.
  • GO:0009253 The chemical reactions and pathways resulting in the breakdown of peptidoglycans, any of a class of glycoconjugates found in bacterial cell walls and consisting of long glycan strands of alternating residues of beta-(1,4) linked N-acetylglucosamine and N-acetylmuramic acid, cross-linked by short peptides.
  • GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
  • GO:0000270 The chemical reactions and pathways involving peptidoglycans, any of a class of glycoconjugates found only in bacterial cell walls and consisting of long glycan strands of alternating residues of beta-(1,4) linked N-acetylglucosamine and N-acetylmuramic acid, cross-linked by short peptides.
  • GO:0016837 Catalysis of the cleavage of a carbon-oxygen bond by the elimination of an alcohol from a polysaccharide.

Sequence Features

Domain/signature hits from InterPro and related databases.

20 records
Show feature table
Start End DB Term Name
1 451 Hamap MF_02016 Membrane-bound lytic murein transglycosylase F [mltF].
1 451 InterPro IPR023703 Membrane-bound lytic murein transglycosylase F
7 230 SUPERFAMILY SSF53850 Periplasmic binding protein-like II
6 231 SMART SM00062 AABind_6
6 231 InterPro IPR001638 Solute-binding protein family 3/N-terminal domain of MltF
274 302 ProSitePatterns PS00922 Prokaryotic transglycosylases signature.
274 302 InterPro IPR000189 Prokaryotic transglycosylase, active site
8 230 Pfam PF00497 Bacterial extracellular solute-binding proteins, family 3
8 230 InterPro IPR001638 Solute-binding protein family 3/N-terminal domain of MltF
208 415 SUPERFAMILY SSF53955 Lysozyme-like
208 415 InterPro IPR023346 Lysozyme-like domain superfamily
257 417 CDD cd13403 MLTF-like
2 225 Gene3D G3DSA:3.40.190.10 -
92 187 Gene3D G3DSA:3.40.190.10 -
257 364 Pfam PF01464 Transglycosylase SLT domain
257 364 InterPro IPR008258 Transglycosylase SLT domain 1
5 229 CDD cd01009 PBP2_YfhD_N
236 418 Gene3D G3DSA:1.10.530.10 -
428 452 MobiDBLite mobidb-lite consensus disorder prediction
246 365 PANTHER PTHR35936 MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE F

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

9 + 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 5AA2
X-ray 2.80 Å A,B,C,D
98.5% 8-452
PDBe RCSB PDBj File
Viewing
PDB 5AA1
X-ray 2.89 Å A,B,C,D
98.5% 8-452
PDBe RCSB PDBj File
Loaded
PDB 5AA3
X-ray 3.20 Å A,B,C,D,E,F,G,H,I,J,K,L
98.5% 8-452
PDBe RCSB PDBj File
Loaded
PDB 4P0G
X-ray 1.65 Å A
94.0% 28-452
PDBe RCSB PDBj File
Loaded
PDB 4P11
X-ray 1.89 Å A
94.0% 28-452
PDBe RCSB PDBj File
Loaded
PDB 4OYV
X-ray 2.31 Å A
94.0% 28-452
PDBe RCSB PDBj File
Loaded
PDB 4OWD
X-ray 2.21 Å A
92.9% 33-452
PDBe RCSB PDBj File
Loaded
PDB 4OZ9
X-ray 2.24 Å A
92.9% 33-452
PDBe RCSB PDBj File
Loaded
PDB 5A5X
X-ray 1.80 Å A
91.8% 38-452
PDBe RCSB PDBj File
Loaded
AlphaFold PA3764
AlphaFold — — full sequence — Loaded
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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.

53 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
6X4
5AA4
A0A1I9GEN8 489.6 Da LogP -3.89 TPSA 244.7 1 viol. ✓ Clean C[C@H](C(=O)N)NC(=O)C(CCCC[NH3+])NC(=O)CC[C@H](…
ORN
3VVD
Q72JG5 132.2 Da LogP -0.86 TPSA 89.3 ✓ Ro5 ✓ Clean C(C[C@@H](C(=O)O)N)CN
SLZ
3VV5
Q72JG5 164.2 Da LogP -0.91 TPSA 89.3 ✓ Ro5 ✓ Clean C(CSC[C@@H](C(=O)O)N)N

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.