Protein profile

PA4392

hypothetical protein

Genome: NC_002516.2

Gene: ALP65_00522 CAZ10_21365 ogt_1 PA4392 PAERUG_P19_London_7_VIM_2_05_10_00272 GNQ48_11155 IPC1295_15670 GUL26_13245 Structure source: AlphaFold UniProt G3XD79 UniProt Q9X3S4
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Amino acids 127
Annotations 3
Features 11
PDB binders 2
Druggability 0.869

Overview

Basic information about this protein and its source genome.

Accession
PA4392
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
ALP65_00522 CAZ10_21365 ogt_1 PA4392 PAERUG_P19_London_7_VIM_2_05_10_00272 GNQ48_11155 IPC1295_15670 GUL26_13245
Status
annotated
Amino acids
127
Structure source
AlphaFold
GO
GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic. GO:0003684 Binding to damaged DNA. GO:0006281 The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
43.333
Human E-value
1.34e-06
Gut microbiome off-target
hit
Essential (DEG)
Y
Localization
Unknown

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 0.869
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

3 GO

Gene Ontology (GO)

3
  • GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
  • GO:0003684 Binding to damaged DNA.
  • GO:0006281 The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.

Sequence Features

Domain/signature hits from InterPro and related databases.

11 records
Show feature table
Start End DB Term Name
24 127 Gene3D G3DSA:1.10.10.10 -
24 127 InterPro IPR036388 Winged helix-like DNA-binding domain superfamily
23 125 PANTHER PTHR42942 6-O-METHYLGUANINE DNA METHYLTRANSFERASE
29 110 SUPERFAMILY SSF46767 Methylated DNA-protein cysteine methyltransferase, C-terminal domain
29 110 InterPro IPR036217 Methylated DNA-protein cysteine methyltransferase, DNA binding domain
29 108 CDD cd06445 ATase
29 108 InterPro IPR014048 Methylated-DNA-[protein]-cysteine S-methyltransferase, DNA binding
29 109 Pfam PF01035 6-O-methylguanine DNA methyltransferase, DNA binding domain
29 109 InterPro IPR014048 Methylated-DNA-[protein]-cysteine S-methyltransferase, DNA binding
1 16 MobiDBLite mobidb-lite consensus disorder prediction
1 22 MobiDBLite mobidb-lite consensus disorder prediction

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 + 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 PA4392
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
1 0.869
3 0.28

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.

52 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
ETW
6GA0
Q97VW7 479.5 Da LogP 5.21 TPSA 116.8 1 viol. ✓ Clean Cc1ccc(cc1)CNC(=O)c2ccc(c(c2)C(=O)O)C3=C4C=CC(=…
PBO
3GYH
Q9UTN9 149.2 Da LogP 2.06 TPSA 30.0 ✓ Ro5 ✓ Clean CCCC(=O)c1cccnc1

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.