Target Pathogen

Overview

Basic information about this protein and its source genome.

Accession: PA4808
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: selA PA4808
Status: annotated
Amino acids: 468
Structure source: AlphaFold

EC

2.9.1.1

GO

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0004125 Catalysis of the reaction: L-seryl-tRNA(Sec) + selenophosphate = L-selenocysteinyl-tRNA(Sec) + H2O + phosphate. GO:0001717 The modification process that results in the conversion of serine, carried by a specialized tRNA(ser) (which can read a UGA anticodon), to selenocysteine. GO:0001514 The incorporation of selenocysteine into a peptide; uses a special tRNA that recognizes the UGA codon as selenocysteine, rather than as a termination codon. Selenocysteine is synthesized from serine before its incorporation; it is not a posttranslational modification of peptidyl-cysteine. 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 0.551

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

Enzyme Commission (EC)

1

2.9.1.1

Gene Ontology (GO)

5

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0004125 Catalysis of the reaction: L-seryl-tRNA(Sec) + selenophosphate = L-selenocysteinyl-tRNA(Sec) + H2O + phosphate.
GO:0001717 The modification process that results in the conversion of serine, carried by a specialized tRNA(ser) (which can read a UGA anticodon), to selenocysteine.
GO:0001514 The incorporation of selenocysteine into a peptide; uses a special tRNA that recognizes the UGA codon as selenocysteine, rather than as a termination codon. Selenocysteine is synthesized from serine before its incorporation; it is not a posttranslational modification of peptidyl-cysteine.
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.

15 records

Show feature table

Start	End	DB	Term	Name
1	464	PANTHER	PTHR32328	L-SERYL-TRNA(SEC) SELENIUM TRANSFERASE
5	42	Pfam	PF12390	Selenocysteine synthase N terminal
5	42	InterPro	IPR025862	L-seryl-tRNA selenium transferase N-terminal domain
1	466	Hamap	MF_00423	L-seryl-tRNA(Sec) selenium transferase [selA].
1	466	InterPro	IPR004534	L-seryl-tRNA(Sec) selenium transferase
91	354	Gene3D	G3DSA:3.40.640.10	-
91	354	InterPro	IPR015421	Pyridoxal phosphate-dependent transferase, major domain
5	455	NCBIfam	TIGR00474	L-seryl-tRNA(Sec) selenium transferase
5	455	InterPro	IPR004534	L-seryl-tRNA(Sec) selenium transferase
77	451	Gene3D	G3DSA:3.90.1150.180	-
91	354	FunFam	G3DSA:3.40.640.10:FF:000028	L-seryl-tRNA(Sec) selenium transferase
74	375	SUPERFAMILY	SSF53383	PLP-dependent transferases
74	375	InterPro	IPR015424	Pyridoxal phosphate-dependent transferase
79	450	Pfam	PF03841	L-seryl-tRNA selenium transferase
79	450	InterPro	IPR018319	L-seryl-tRNA selenium transferase-like

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

Loading 3D structure...

Legend High Medium Low

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 PA4808	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
6				0.551
2				0.233

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.

1 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.

No PDB structure with a co-crystallized ligand found for this exact protein.

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.

Ligand	Source crystal	UniProt (homolog)	MW · LogP · TPSA	Lipinski	PAINS	SMILES
THJ	3W1J	O67140	112.1 Da LogP -1.01 TPSA 57.2	✓ Ro5	✓ Clean	`[O-]S(=O)(=O)[S-]`

Experimental bioactivity from ChEMBL measured directly on this protein. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL bioactivity data found for this exact protein.

Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL hits found through similar proteins.

Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).

No virtual-screening candidates for this protein.

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.

PA4808