Target Pathogen

Overview

Basic information about this protein and its source genome.

Accession: PA4729
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: panB
Status: annotated
Amino acids: 266
Structure source: ColabFold

GO

GO:0015940 The chemical reactions and pathways resulting in the formation of pantothenate, the anion of pantothenic acid. It is a B complex vitamin that is a constituent of coenzyme A and is distributed ubiquitously in foods. 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:0003864 Catalysis of the reaction: 5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate = tetrahydrofolate + 2-dehydropantoate.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
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 0.781

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:0015940 The chemical reactions and pathways resulting in the formation of pantothenate, the anion of pantothenic acid. It is a B complex vitamin that is a constituent of coenzyme A and is distributed ubiquitously in foods.
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:0003864 Catalysis of the reaction: 5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate = tetrahydrofolate + 2-dehydropantoate.

Sequence Features

Domain/signature hits from InterPro and related databases.

16 records

Show feature table

Start	End	DB	Term	Name
4	264	Hamap	MF_00156	3-methyl-2-oxobutanoate hydroxymethyltransferase [panB].
4	264	InterPro	IPR003700	Ketopantoate hydroxymethyltransferase
2	266	PIRSF	PIRSF000388	PanB
2	266	InterPro	IPR003700	Ketopantoate hydroxymethyltransferase
6	258	CDD	cd06557	KPHMT-like
6	258	InterPro	IPR003700	Ketopantoate hydroxymethyltransferase
1	264	Gene3D	G3DSA:3.20.20.60	-
1	264	InterPro	IPR040442	Pyruvate kinase-like domain superfamily
2	264	PANTHER	PTHR20881	3-METHYL-2-OXOBUTANOATE HYDROXYMETHYLTRANSFERASE
2	264	InterPro	IPR003700	Ketopantoate hydroxymethyltransferase
4	259	Pfam	PF02548	Ketopantoate hydroxymethyltransferase
4	259	InterPro	IPR003700	Ketopantoate hydroxymethyltransferase
1	266	FunFam	G3DSA:3.20.20.60:FF:000003	3-methyl-2-oxobutanoate hydroxymethyltransferase
4	264	NCBIfam	TIGR00222	3-methyl-2-oxobutanoate hydroxymethyltransferase
4	264	SUPERFAMILY	SSF51621	Phosphoenolpyruvate/pyruvate domain
4	264	InterPro	IPR015813	Pyruvate/Phosphoenolpyruvate kinase-like domain superfamily

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
ColabFold PA4729	ColabFold	—	—	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				0.781

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.

2 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
KIV	1O68	Q9JZW6	116.1 Da LogP 0.30 TPSA 54.4	✓ Ro5	✓ Clean	`CC(C)C(=O)C(=O)O`
KPL	1M3U	P31057	146.1 Da LogP -0.34 TPSA 74.6	✓ Ro5	✓ Clean	`CC(C)(CO)C(=O)C(=O)O`

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.

PA4729