Overview
Basic information about this protein and its source genome.
- Accession
- PA0008
- Gene
- PA0008 glyS
- Status
- annotated
- Amino acids
- 684
- Structure source
- AlphaFold
Target profile
Computed evidence for target prioritization.
- Human off-target
- No hit
- Gut microbiome off-target
- hit
- Essential (DEG)
- Y
- 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.
Sequence
Primary amino-acid sequence viewer.
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Enzyme Commission (EC)
1Gene Ontology (GO)
8- GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
- GO:0004814 Catalysis of the reaction: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg).
- GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
- GO:0004820 Catalysis of the reaction: ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly).
- GO:0006420 The process of coupling arginine to arginyl-tRNA, catalyzed by arginyl-tRNA synthetase. The arginyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of an alanine accetping tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification.
- GO:0006426 The process of coupling glycine to glycyl-tRNA, catalyzed by glycyl-tRNA synthetase. The glycyll-tRNA synthetase is a class-II synthetase. The activated amino acid is transferred to the 3'-OH group of a glycine-accepting tRNA.
- GO:0000166 Binding to a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose.
- GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 334 | 485 | SUPERFAMILY | SSF109604 | HD-domain/PDEase-like |
| 5 | 683 | NCBIfam | TIGR00211 | glycine--tRNA ligase subunit beta |
| 5 | 683 | InterPro | IPR015944 | Glycine-tRNA ligase, beta subunit |
| 6 | 544 | Pfam | PF02092 | Glycyl-tRNA synthetase beta subunit |
| 6 | 544 | InterPro | IPR015944 | Glycine-tRNA ligase, beta subunit |
| 3 | 683 | Hamap | MF_00255 | Glycine--tRNA ligase beta subunit [glyS]. |
| 3 | 683 | InterPro | IPR015944 | Glycine-tRNA ligase, beta subunit |
| 358 | 648 | ProSiteProfiles | PS50861 | Heterodimeric glycyl-transfer RNA synthetases family profile. |
| 358 | 648 | InterPro | IPR006194 | Glycine-tRNA synthetase, heterodimeric |
| 577 | 671 | Pfam | PF05746 | DALR anticodon binding domain |
| 577 | 671 | InterPro | IPR008909 | DALR anticodon binding |
| 3 | 683 | PANTHER | PTHR30075 | GLYCYL-TRNA SYNTHETASE |
| 3 | 683 | InterPro | IPR006194 | Glycine-tRNA synthetase, heterodimeric |
| 580 | 683 | SMART | SM00836 | dalr_1_4 |
| 580 | 683 | InterPro | IPR008909 | DALR anticodon binding |
| 241 | 256 | PRINTS | PR01045 | Glycyl-tRNA synthetase beta subunit signature |
| 241 | 256 | InterPro | IPR015944 | Glycine-tRNA ligase, beta subunit |
| 313 | 329 | PRINTS | PR01045 | Glycyl-tRNA synthetase beta subunit signature |
| 313 | 329 | InterPro | IPR015944 | Glycine-tRNA ligase, beta subunit |
| 7 | 20 | PRINTS | PR01045 | Glycyl-tRNA synthetase beta subunit signature |
| 7 | 20 | InterPro | IPR015944 | Glycine-tRNA ligase, beta subunit |
| 389 | 408 | PRINTS | PR01045 | Glycyl-tRNA synthetase beta subunit signature |
| 389 | 408 | InterPro | IPR015944 | Glycine-tRNA ligase, beta subunit |
| 50 | 62 | PRINTS | PR01045 | Glycyl-tRNA synthetase beta subunit signature |
| 50 | 62 | InterPro | IPR015944 | Glycine-tRNA ligase, beta subunit |
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...
Structural evidence
0 + 1Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold
PA0008
|
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 |
|---|---|---|---|---|---|---|---|
| 5 | 0.812 | ||||||
| 2 | 0.583 | ||||||
| 1 | 0.361 | ||||||
| 12 | 0.202 |