Protein profile

PA5177

hydrolase

Genome: NC_002516.2

Gene: PA5177 Structure source: AlphaFold UniProt Q9HU12
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Amino acids 221
Annotations 4
Features 21
PDB binders 2
Druggability 0.62

Overview

Basic information about this protein and its source genome.

Accession
PA5177
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA5177
Status
annotated
Amino acids
221
Structure source
AlphaFold
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:0046872 Binding to a metal ion. GO:0008967 Catalysis of the reaction: 2-phosphoglycolate + H2O = glycolate + 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.

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 0.62
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

4 GO

Gene Ontology (GO)

4
  • GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
  • GO:0046872 Binding to a metal ion.
  • GO:0008967 Catalysis of the reaction: 2-phosphoglycolate + H2O = glycolate + 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.

Sequence Features

Domain/signature hits from InterPro and related databases.

21 records
Show feature table
Start End DB Term Name
5 203 SUPERFAMILY SSF56784 HAD-like
5 203 InterPro IPR036412 HAD-like superfamily
91 186 NCBIfam TIGR01509 HAD-IA family hydrolase
91 186 InterPro IPR006439 HAD hydrolase, subfamily IA
8 204 Gene3D G3DSA:3.40.50.1000 -
8 204 InterPro IPR023214 HAD superfamily
153 173 PRINTS PR00413 Haloacid dehalogenase/epoxide hydrolase family signature
153 173 InterPro IPR006439 HAD hydrolase, subfamily IA
9 20 PRINTS PR00413 Haloacid dehalogenase/epoxide hydrolase family signature
9 20 InterPro IPR006439 HAD hydrolase, subfamily IA
104 117 PRINTS PR00413 Haloacid dehalogenase/epoxide hydrolase family signature
104 117 InterPro IPR006439 HAD hydrolase, subfamily IA
135 151 PRINTS PR00413 Haloacid dehalogenase/epoxide hydrolase family signature
135 151 InterPro IPR006439 HAD hydrolase, subfamily IA
180 193 PRINTS PR00413 Haloacid dehalogenase/epoxide hydrolase family signature
180 193 InterPro IPR006439 HAD hydrolase, subfamily IA
10 196 PANTHER PTHR43434 PHOSPHOGLYCOLATE PHOSPHATASE
10 217 SFLD SFLDG01129 C1.5: HAD, Beta-PGM, Phosphatase Like
12 187 Pfam PF13419 Haloacid dehalogenase-like hydrolase
12 187 InterPro IPR041492 Haloacid dehalogenase-like hydrolase
10 217 SFLD SFLDS00003 Haloacid Dehalogenase

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
AlphaFold PA5177
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 0.62

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.

35 records

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.

Show only:
Ligand Source crystal UniProt (homolog) MW · LogP · TPSA Lipinski PAINS SMILES
NHE
4YGR
B6YTD6 207.3 Da LogP 0.80 TPSA 66.4 ✓ Ro5 ✓ Clean C1CCC(CC1)NCCS(=O)(=O)O
TBU
4YGQ
B6YTD6 74.1 Da LogP 0.78 TPSA 20.2 ✓ Ro5 ✓ Clean CC(C)(C)O

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.