Target Pathogen

Overview

Basic information about this protein and its source genome.

Accession: PA1311
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: phnX PA1311
Status: annotated
Amino acids: 275
Structure source: AlphaFold

EC

3.11.1.1

GO

GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0000287 Binding to a magnesium (Mg) ion. GO:0008967 Catalysis of the reaction: 2-phosphoglycolate + H2O = glycolate + phosphate. GO:0050194 Catalysis of the reaction: H2O + phosphonoacetaldehyde = acetaldehyde + H+ + phosphate. 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. GO:0019700 The chemical reactions and pathways resulting in the breakdown of phosphonates, any organic compound containing one or more C-PO(OH)2 or C-PO(OR)2 (with R=alkyl, aryl) groups. Catabolism of phosphonic acid itself, an inorganic compound without the biochemically relevant C-P bond, is not included.

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 0.686

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MNYNQPATLQAAILDWAGTVVDFGSFAPTQIFVEAFAEFGVQVSLEEARGPMGMGKWDHIRTLCDIPAIAERYRAVFGRLPSDDDVTAIYERFMPLQIEKIAEHSALIPGALQAIAELRGMGLKIGSCSGYPAVVMEKVVALAETNGYVADHVVATDEVPNGRPWPAQALANVIALGIDDVAACVKVDDTWPGILEGRRAGMWTVALTCSGNALGLTYEQYQALPAAELERERTRIEQMFEGSRPHYLIETIAELPAVVRDINARLARGEMPQGN

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

1

3.11.1.1

Gene Ontology (GO)

6

GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0000287 Binding to a magnesium (Mg) ion.
GO:0008967 Catalysis of the reaction: 2-phosphoglycolate + H2O = glycolate + phosphate.
GO:0050194 Catalysis of the reaction: H2O + phosphonoacetaldehyde = acetaldehyde + H+ + phosphate.
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.
GO:0019700 The chemical reactions and pathways resulting in the breakdown of phosphonates, any organic compound containing one or more C-PO(OH)2 or C-PO(OR)2 (with R=alkyl, aryl) groups. Catabolism of phosphonic acid itself, an inorganic compound without the biochemically relevant C-P bond, is not included.

Sequence Features

Domain/signature hits from InterPro and related databases.

19 records

Show feature table

Start	End	DB	Term	Name
14	201	Pfam	PF00702	haloacid dehalogenase-like hydrolase
1	272	SFLD	SFLDF00038	phosphonoacetaldehyde hydrolase
10	262	SUPERFAMILY	SSF56784	HAD-like
10	262	InterPro	IPR036412	HAD-like superfamily
1	272	SFLD	SFLDS00003	Haloacid Dehalogenase
10	257	PANTHER	PTHR43434	PHOSPHOGLYCOLATE PHOSPHATASE
9	259	NCBIfam	TIGR01422	phosphonoacetaldehyde hydrolase
9	259	InterPro	IPR006323	Phosphonoacetaldehyde hydrolase
1	275	Hamap	MF_01375	Phosphonoacetaldehyde hydrolase [phnX].
1	275	InterPro	IPR006323	Phosphonoacetaldehyde hydrolase
27	104	Gene3D	G3DSA:1.10.150.240	Putative phosphatase; domain 2
27	104	InterPro	IPR023198	Phosphoglycolate phosphatase-like, domain 2
11	269	Gene3D	G3DSA:3.40.50.1000	-
11	269	InterPro	IPR023214	HAD superfamily
27	104	FunFam	G3DSA:1.10.150.240:FF:000006	Phosphonoacetaldehyde hydrolase
81	206	NCBIfam	TIGR01509	HAD-IA family hydrolase
81	206	InterPro	IPR006439	HAD hydrolase, subfamily IA
9	250	CDD	cd02586	HAD_PHN
9	250	InterPro	IPR006323	Phosphonoacetaldehyde hydrolase

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 PA1311	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
4				0.686
2				0.434

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.

5 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
ESA	1RDF	O31156	110.1 Da LogP -0.11 TPSA 54.4	✓ Ro5	✓ Clean	`CCS(=O)(=O)O`
PGA	1TE2	P77247	156.0 Da LogP -0.82 TPSA 104.1	✓ Ro5	✓ Clean	`C(C(=O)O)OP(=O)(O)O`
POA	1SWW	O31156	124.0 Da LogP -0.64 TPSA 74.6	✓ Ro5	✓ Clean	`C(C=O)P(=O)(O)O`
VSO	1RQL	O31156	108.1 Da LogP 0.02 TPSA 54.4	✓ Ro5	✓ Clean	`C=CS(=O)(=O)O`
WO4	1FEZ	O31156	247.8 Da LogP -2.62 TPSA 80.3	✓ Ro5	✓ Clean	`[O-][W](=O)(=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.

PA1311