Protein profile

PA1346

hypothetical protein

Genome: NC_002516.2

Gene: PA1346 Structure source: AlphaFold UniProt Q9I3Z8
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Amino acids 515
Annotations 4
Features 16
PDB binders 1
Druggability 0.741

Overview

Basic information about this protein and its source genome.

Accession
PA1346
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA1346
Status
annotated
Amino acids
515
Structure source
AlphaFold
GO
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0016831 Catalysis of the nonhydrolytic addition or removal of a carboxyl group to or from a compound. GO:0006520 The chemical reactions and pathways involving amino acids, carboxylic acids containing one or more amino groups. 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.

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 0.741
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

MSRNNPSRHSILVTSNINAANDANRLSELCRQLEIRGYRLFQAPSRKVALDFLGNAAHPAGILLLVAEPTGENEAAQLAALDELRQVAPSIPLFLLFRQLRIEQLSSQLLDEAQGCFNLAAGPARFIAERIDSDLREWRAPAGPRRLRDYAPPVPRTPVSARYNGRARLDLAPAKQWRIGSGSTAERLATPLNDLSTAYRKTSAGAPAAHAGDIAEAFRRALWEAAARLAREDGDTWFFEILRGNPGPGIEAGRETPAKRWHGLAETLDSSPRLDPLRVALSAPGLDSRGRPASFGVPAAVVCRYLRRHGIAPLRTGDYRFLLLFPQGARAEHAQPLVDRLCEFKRRHDDDAPLKQVLPELLDSSPLYRYIGLRELCAMIHEASLRLHLTALADAAARAAGHAALAPATVYGHLVRDETEAVAIDRLGGRVVASLVGVHPAATPLLLPGERVAEESPALIDYLLALQAFGEHFPGFAPELQGIEIDERGRYRVRCVRPAALARGSGLRLATRRPD

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

4 GO

Gene Ontology (GO)

4
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0016831 Catalysis of the nonhydrolytic addition or removal of a carboxyl group to or from a compound.
  • GO:0006520 The chemical reactions and pathways involving amino acids, carboxylic acids containing one or more amino groups.
  • 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.

Sequence Features

Domain/signature hits from InterPro and related databases.

16 records
Show feature table
Start End DB Term Name
358 487 Pfam PF03711 Orn/Lys/Arg decarboxylase, C-terminal domain
358 487 InterPro IPR008286 Orn/Lys/Arg decarboxylase, C-terminal
256 330 Pfam PF01276 Orn/Lys/Arg decarboxylase, major domain
256 330 InterPro IPR000310 Orn/Lys/Arg decarboxylase, major domain
10 141 Gene3D G3DSA:3.40.50.2300 -
256 494 PANTHER PTHR45229 CONSTITUTIVE ORNITHINE DECARBOXYLASE
256 494 InterPro IPR011193 Ornithine/lysine/arginine decarboxylase
25 136 Pfam PF03709 Orn/Lys/Arg decarboxylase, N-terminal domain
25 136 InterPro IPR005308 Orn/Lys/Arg decarboxylase, N-terminal
353 496 SUPERFAMILY SSF55904 Ornithine decarboxylase C-terminal domain
353 496 InterPro IPR036633 Orn/Lys/Arg decarboxylase, C-terminal domain superfamily
378 498 Gene3D G3DSA:3.90.100.10 -
212 377 Gene3D G3DSA:3.90.1150.10 Aspartate Aminotransferase, domain 1
212 377 InterPro IPR015422 Pyridoxal phosphate-dependent transferase, small domain
235 350 SUPERFAMILY SSF53383 PLP-dependent transferases
235 350 InterPro IPR015424 Pyridoxal phosphate-dependent transferase

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 PA1346
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 0.339
2 0.314

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.

51 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
G4P
3N75
P0A9H3 603.2 Da LogP -2.22 TPSA 345.6 3 viol. ✓ Clean c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=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.