Protein profile

PA3853

transferase

Genome: NC_002516.2

Gene: PA3853 Structure source: AlphaFold UniProt Q9HXF3
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Amino acids 229
Annotations 7
Features 9
PDB binders 6
Druggability 0.539

Overview

Basic information about this protein and its source genome.

Accession
PA3853
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA3853
Status
annotated
Amino acids
229
Structure source
AlphaFold
EC
2.3.1.28
GO
GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. GO:0016407 Catalysis of the transfer of an acetyl group to an acceptor molecule. GO:0008811 Catalysis of the reaction: chloramphenicol + acetyl-CoA = chloramphenicol 3-acetate + CoA. GO:0009245 The chemical reactions and pathways resulting in the formation of lipid A, the glycolipid group of bacterial lipopolysaccharides, consisting of four to six fatty acyl chains linked to two glucosamine residues. Further modifications of the backbone are common. GO:0046677 Any process that results in a change in state or activity of a cell or an organism (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:0016740 Catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2.

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
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 0.539
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

6
  • GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
  • GO:0016407 Catalysis of the transfer of an acetyl group to an acceptor molecule.
  • GO:0008811 Catalysis of the reaction: chloramphenicol + acetyl-CoA = chloramphenicol 3-acetate + CoA.
  • GO:0009245 The chemical reactions and pathways resulting in the formation of lipid A, the glycolipid group of bacterial lipopolysaccharides, consisting of four to six fatty acyl chains linked to two glucosamine residues. Further modifications of the backbone are common.
  • GO:0046677 Any process that results in a change in state or activity of a cell or an organism (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:0016740 Catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2.

Sequence Features

Domain/signature hits from InterPro and related databases.

9 records
Show feature table
Start End DB Term Name
43 197 Gene3D G3DSA:2.160.10.10 Hexapeptide repeat proteins
39 186 PANTHER PTHR43300 ACETYLTRANSFERASE
34 192 SUPERFAMILY SSF51161 Trimeric LpxA-like enzymes
34 192 InterPro IPR011004 Trimeric LpxA-like superfamily
50 187 CDD cd03349 LbH_XAT
124 152 ProSitePatterns PS00101 Hexapeptide-repeat containing-transferases signature.
124 152 InterPro IPR018357 Hexapeptide transferase, conserved site
116 150 Pfam PF00132 Bacterial transferase hexapeptide (six repeats)
116 150 InterPro IPR001451 Hexapeptide repeat

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 PA3853
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
9 0.539
6 0.264
7 0.22

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.

56 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
B2M
3DHO
P50870 453.1 Da LogP 5.08 TPSA 74.6 1 viol. Alert Cc1cc(c2cc(ccc2n1)Br)C(=O)N/N=C\c3cc(cc(c3O)Cl)…
DCA
2XAT
P26841 735.5 Da LogP -1.58 TPSA 346.6 3 viol. ✓ Clean CCNC(=O)CCNC(=O)[C@@H](C(C)(C)CO[P@@](=O)(O)O[P…
DOL
1MRL
P50870 690.9 Da LogP 2.27 TPSA 176.4 2 viol. ✓ Clean CCN(CC)CCS(=O)(=O)[C@@H]1CCN2[C@H]1C(=O)O[C@@H]…
SXA
6X3C
P26839 400.4 Da LogP -0.61 TPSA 162.3 ✓ Ro5 ✓ Clean CC(=O)SCCNC(=O)CCNC(=O)[C@H](C(C)(C)COP(=O)(O)O…
T3F
3FSC
Q6TFC6 547.3 Da LogP -2.46 TPSA 262.3 3 viol. ✓ Clean C[C@@H]1[C@@H]([C@@H]([C@H]([C@H](O1)O[P@@](=O)…
T3Q
3FSB
Q6TFC6 547.3 Da LogP -2.46 TPSA 262.3 3 viol. ✓ Clean C[C@@H]1[C@H]([C@@H]([C@H]([C@H](O1)O[P@](=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.