Protein profile

PA1757

phosphoserine phosphatase

Genome: NC_002516.2

Gene: PA1757 thrH Structure source: Experimental + AlphaFold UniProt Q9I2Y2
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Amino acids 205
Annotations 10
Features 10
PDB binders 0
Druggability 0.79

Overview

Basic information about this protein and its source genome.

Accession
PA1757
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA1757 thrH
Status
annotated
Amino acids
205
Structure source
Experimental + AlphaFold
EC
3.1.3.3
GO
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0046820 Catalysis of the reaction: L-glutamine + chorismate = 4-amino-4-deoxychorismate + L-glutamate. It is composed of two enzymatic activities (which may be present on one or two polypeptides); the first is a glutaminase which yields ammonia from glutamine, releasing glutamate. The ammonia is used by the second activity which catalyzes the amination of chorismate to form 4-amino-4-deoxychorismate. GO:0036424 Catalysis of the reaction: O-phospho-L-serine + H2O = L-serine + phosphate, on a free amino acid. GO:0000287 Binding to a magnesium (Mg) ion. GO:0043899 Catalysis of the transfer of a phosphoryl group from phosphoserine to homoserine to form phosphohomoserine. GO:0016311 The process of removing one or more phosphoric (ester or anhydride) residues from a molecule.

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 0.79
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

9
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0046820 Catalysis of the reaction: L-glutamine + chorismate = 4-amino-4-deoxychorismate + L-glutamate. It is composed of two enzymatic activities (which may be present on one or two polypeptides); the first is a glutaminase which yields ammonia from glutamine, releasing glutamate. The ammonia is used by the second activity which catalyzes the amination of chorismate to form 4-amino-4-deoxychorismate.
  • GO:0036424 Catalysis of the reaction: O-phospho-L-serine + H2O = L-serine + phosphate, on a free amino acid.
  • GO:0000287 Binding to a magnesium (Mg) ion.
  • GO:0043899 Catalysis of the transfer of a phosphoryl group from phosphoserine to homoserine to form phosphohomoserine.
  • GO:0016311 The process of removing one or more phosphoric (ester or anhydride) residues from a molecule.
  • GO:0006564 The chemical reactions and pathways resulting in the formation of L-serine.
  • GO:0046654 The chemical reactions and pathways resulting in the formation of tetrahydrofolate, 5,6,7,8-tetrahydrofolic acid, a folate derivative bearing additional hydrogens on the pterin group.
  • GO:0009088 The chemical reactions and pathways resulting in the formation of L-threonine (2-amino-3-hydroxybutyric acid), a polar, uncharged, essential amino acid found in peptide linkage in proteins.

Sequence Features

Domain/signature hits from InterPro and related databases.

10 records
Show feature table
Start End DB Term Name
64 160 Pfam PF12710 haloacid dehalogenase-like hydrolase
1 203 NCBIfam TIGR02137 bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH
1 203 InterPro IPR011863 Phosphoserine phosphatase/homoserine phosphotransferase bifunctional protein
2 191 SUPERFAMILY SSF56784 HAD-like
2 191 InterPro IPR036412 HAD-like superfamily
13 128 Gene3D G3DSA:3.90.1470.10 thrh gene product, domain 2
3 191 Gene3D G3DSA:3.40.50.1000 -
3 191 InterPro IPR023214 HAD superfamily
1 195 CDD cd02607 HAD_ThrH_like
32 173 PANTHER PTHR43344 PHOSPHOSERINE PHOSPHATASE

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

2 + 1

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry Method Resolution Chain Coverage Links Status
PDB 1RKU
X-ray 1.47 Å A,B
100.0% 1-205
PDBe RCSB PDBj File
Viewing
PDB 1RKV
X-ray 1.90 Å A,B
100.0% 1-205
PDBe RCSB PDBj File
Loaded
AlphaFold PA1757
AlphaFold — — full sequence — Loaded
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
5 0.79
2 0.435
1 0.205

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK Sticks Spheres Surfaces Score Probability Labels Zoom Positions
1 14.38 0.721
2 1.17 0.01