Target Pathogen

Overview

Basic information about this protein and its source genome.

Accession: PA5228
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA5228
Status: annotated
Amino acids: 203
Structure source: AlphaFold

EC

6.3.3.2

GO

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0030272 Catalysis of the reaction: 5-formyltetrahydrofolate + ATP = 5,10-methenyltetrahydrofolate + ADP + H+ + phosphate. GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0046872 Binding to a metal ion. GO:0009396 The chemical reactions and pathways resulting in the formation of folic acid and its derivatives. GO:0035999 The chemical reactions and pathways by which one-carbon (C1) units are transferred between tetrahydrofolate molecules, to synthesize other tetrahydrofolate molecules.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 27.027
Human E-value: 9.01e-15
Gut microbiome off-target: hit
Essential (DEG): N
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 0.805

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

6.3.3.2

Gene Ontology (GO)

6

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0030272 Catalysis of the reaction: 5-formyltetrahydrofolate + ATP = 5,10-methenyltetrahydrofolate + ADP + H+ + phosphate.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0046872 Binding to a metal ion.
GO:0009396 The chemical reactions and pathways resulting in the formation of folic acid and its derivatives.
GO:0035999 The chemical reactions and pathways by which one-carbon (C1) units are transferred between tetrahydrofolate molecules, to synthesize other tetrahydrofolate molecules.

Sequence Features

Domain/signature hits from InterPro and related databases.

12 records

Show feature table

Start	End	DB	Term	Name
11	193	NCBIfam	TIGR02727	5-formyltetrahydrofolate cyclo-ligase
11	193	InterPro	IPR002698	5-formyltetrahydrofolate cyclo-ligase
11	193	Pfam	PF01812	5-formyltetrahydrofolate cyclo-ligase family
8	200	SUPERFAMILY	SSF100950	NagB/RpiA/CoA transferase-like
8	200	InterPro	IPR037171	NagB/RpiA transferase-like
3	201	FunFam	G3DSA:3.40.50.10420:FF:000009	5-formyltetrahydrofolate cyclo-ligase
3	201	Gene3D	G3DSA:3.40.50.10420	-
3	201	InterPro	IPR024185	5-formyltetrahydrofolate cyclo-ligase-like domain superfamily
7	196	PIRSF	PIRSF006806	5_FTHF
7	196	InterPro	IPR002698	5-formyltetrahydrofolate cyclo-ligase
11	197	PANTHER	PTHR23407	ATPASE INHIBITOR/5-FORMYLTETRAHYDROFOLATE CYCLO-LIGASE
11	197	InterPro	IPR002698	5-formyltetrahydrofolate cyclo-ligase

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...

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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 PA5228	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				0.805

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.

4 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
10F	3HY3	P49914	479.5 Da LogP -3.29 TPSA 218.4	1 viol.	✓ Clean	`c1cc(ccc1C(=O)N[C@H](CCC(=O)O)C(=O)O)N(C[C@@H]2…`
N5G	3HY4	P49914	567.5 Da LogP -3.64 TPSA 268.1	3 viol.	✓ Clean	`C1CC(CCC1C(=O)N[C@@H](CCC(=O)O)C(=O)O)NC[C@H]2C…`

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).

Ligand	Tanimoto	MW · LogP · TPSA	Lipinski	PAINS	SMILES
ZINC8536462	0.549	473.4 Da LogP -0.73 TPSA 219.8	1 viol.	✓ Clean	`Nc1nc(=O)c2c([nH]1)NC[C@H](CN(C=O)c1ccc(C(=O)N[…`
ZINC4228247	0.542	473.4 Da LogP -0.73 TPSA 219.8	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N[C@H](CN(C=O)c1ccc(C(=O)N[C…`

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.

PA5228