Protein profile
PA4484
aspartyl/glutamyl-tRNA amidotransferase subunit B
Genome: NC_002516.2
Amino acids
481
Annotations
9
Features
23
PDB binders
0
Druggability
0.7
Overview
Basic information about this protein and its source genome.
- Accession
- PA4484
- Gene
- gatB PA4484
- Status
- annotated
- Amino acids
- 481
- Structure source
- Experimental + AlphaFold
EC
GO
GO:0050566 Catalysis of the reaction: L-glutamine + aspartyl-tRNA(Asn) + ATP = L-glutamate + asparaginyl-tRNA(Asn) + phosphate + ADP.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0050567 Catalysis of the reaction: L-glutamine + glutamyl-tRNA(Gln) + ATP = L-glutamate + glutaminyl-tRNA(Gln) + phosphate + ADP.
GO:0070681 A tRNA aminoacylation process in which glutaminyl-tRNAGln is formed by a tRNA-dependent two-step pathway. In the first step a non-discriminating glutamyl-tRNAGlx synthetase generates the misacylated L-glutamyl-tRNAGln species, and in the second step it is amidated to the correctly charged L-glutaminyl-tRNAGln by a glutamyl-tRNAGln amidotransferase.
GO:0006412 The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA or circRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA or circRNA. Translation ends with the release of a polypeptide chain from the ribosome.
GO:0016884 Catalysis of the transfer of the amide nitrogen of glutamine to a substrate. Usually composed of two subunits or domains, one that first hydrolyzes glutamine, and then transfers the resulting ammonia to the second subunit (or domain), where it acts as a source of nitrogen.
Target profile
Computed evidence for target prioritization.
- Human off-target
- hit
- Human identity (%)
- 54.167
- Human E-value
- 4.03e-12
- 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.
FPocket
0.7
Sequence
Primary amino-acid sequence viewer.
MQWETVIGLEIHAQLATQSKIFSGSSTAFGAAPNTQASLVDLAMPGTLPVLNEEAVRMACLFGLAIDARIDRQNVFARKNYFYPDLPKGYQTSQMDHPIVGKGHLDITLEDGTTKRIGITRAHLEEDAGKSLHEDFQGMSGIDLNRAGTPLLEIVSEPDIRSAKEAVAYVKAIHALVRYLGICDGNMAEGSLRCDCNVSVRPKGQAEFGTRAEIKNVNSFRFIEKAINHEIQRQIELIEDGGKVVQETRLYDPNKDETRSMRGKEEANDYRYFPCPDLLPVVIEPEYLAKLREQLPELPVQKRERFESQYGLSAYDASVLSASREMADYFEKVQGICGDAKLAANWVMVELGSLLNKDGLEIEQSPVSAEQLGGMILRIKDNTISGKLAKMVFEAMANGEGSADQIIEAKGLKQVTDSGAIEKMLDEVLAANAEQVEQYRAADEAKRGKMFGFFVGQAMKASKGKANPQQVNELLKKKLEA
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
1 EC
8 GO
Enzyme Commission (EC)
1Gene Ontology (GO)
8- GO:0050566 Catalysis of the reaction: L-glutamine + aspartyl-tRNA(Asn) + ATP = L-glutamate + asparaginyl-tRNA(Asn) + phosphate + ADP.
- GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
- GO:0050567 Catalysis of the reaction: L-glutamine + glutamyl-tRNA(Gln) + ATP = L-glutamate + glutaminyl-tRNA(Gln) + phosphate + ADP.
- GO:0070681 A tRNA aminoacylation process in which glutaminyl-tRNAGln is formed by a tRNA-dependent two-step pathway. In the first step a non-discriminating glutamyl-tRNAGlx synthetase generates the misacylated L-glutamyl-tRNAGln species, and in the second step it is amidated to the correctly charged L-glutaminyl-tRNAGln by a glutamyl-tRNAGln amidotransferase.
- GO:0006412 The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA or circRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA or circRNA. Translation ends with the release of a polypeptide chain from the ribosome.
- GO:0016884 Catalysis of the transfer of the amide nitrogen of glutamine to a substrate. Usually composed of two subunits or domains, one that first hydrolyzes glutamine, and then transfers the resulting ammonia to the second subunit (or domain), where it acts as a source of nitrogen.
- GO:0016874 Catalysis of the joining of two molecules, or two groups within a single molecule, using the energy from the hydrolysis of ATP, a similar triphosphate, or a pH gradient.
- GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
Sequence Features
Domain/signature hits from InterPro and related databases.
23 records
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 4 | 296 | SUPERFAMILY | SSF55931 | Glutamine synthetase/guanido kinase |
| 4 | 296 | InterPro | IPR014746 | Glutamine synthetase/guanido kinase, catalytic domain |
| 2 | 480 | Hamap | MF_00121 | Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B [gatB]. |
| 2 | 480 | InterPro | IPR004413 | Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B |
| 5 | 288 | Pfam | PF02934 | GatB/GatE catalytic domain |
| 5 | 288 | InterPro | IPR006075 | Aspartyl/Glutamyl-tRNA(Gln) amidotransferase, subunit B/E, catalytic |
| 328 | 479 | Pfam | PF02637 | GatB domain |
| 328 | 479 | InterPro | IPR018027 | Asn/Gln amidotransferase |
| 297 | 402 | SUPERFAMILY | SSF89095 | GatB/YqeY motif |
| 297 | 402 | InterPro | IPR003789 | Aspartyl/glutamyl-tRNA amidotransferase subunit B-like |
| 2 | 479 | NCBIfam | TIGR00133 | Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatB |
| 2 | 479 | InterPro | IPR004413 | Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B |
| 328 | 479 | SMART | SM00845 | gatb_yqey_2 |
| 144 | 158 | ProSitePatterns | PS01234 | Glutamyl-tRNA(Gln) amidotransferase subunit B signature. |
| 144 | 158 | InterPro | IPR017958 | Glutamyl-tRNA(Gln) amidotransferase, subunit B, conserved site |
| 296 | 352 | Gene3D | G3DSA:1.10.150.380 | - |
| 296 | 352 | InterPro | IPR042114 | Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, C-terminal, domain 1 |
| 2 | 480 | PANTHER | PTHR11659 | GLUTAMYL-TRNA GLN AMIDOTRANSFERASE SUBUNIT B MITOCHONDRIAL AND PROKARYOTIC PET112-RELATED |
| 2 | 480 | InterPro | IPR017959 | Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, subunit B /E |
| 296 | 351 | FunFam | G3DSA:1.10.150.380:FF:000001 | Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B |
| 415 | 481 | Gene3D | G3DSA:1.10.10.410 | - |
| 415 | 481 | InterPro | IPR023168 | Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, C-terminal, domain 2 |
| 415 | 480 | FunFam | G3DSA:1.10.10.410:FF:000001 | Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B |
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
1 + 1Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer
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 | 15.04 | 0.743 | ||||||
| 2 | 2.29 | 0.058 | ||||||
| 3 | 1.72 | 0.03 | ||||||
| 4 | 1.72 | 0.03 | ||||||
| 5 | 0.94 | 0.005 |
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 | 0.7 | ||||||
| 2 | 0.442 | ||||||
| 3 | 0.261 |
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.
46 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.
No PDB ligands found through similar proteins.
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 |
|---|---|---|---|---|---|
| ZINC1709621 | 0.600 | 248.2 Da LogP -2.17 TPSA 167.0 | ✓ Ro5 | ✓ Clean |
N[C@@H](CC(=O)N[C@@H](CC(=O)O)C(=O)O)C(=O)O
|
| ZINC1709622 | 0.600 | 248.2 Da LogP -2.17 TPSA 167.0 | ✓ Ro5 | ✓ Clean |
N[C@H](CC(=O)N[C@@H](CC(=O)O)C(=O)O)C(=O)O
|
| ZINC1709623 | 0.600 | 248.2 Da LogP -2.17 TPSA 167.0 | ✓ Ro5 | ✓ Clean |
N[C@@H](CC(=O)N[C@H](CC(=O)O)C(=O)O)C(=O)O
|
| ZINC1709624 | 0.600 | 248.2 Da LogP -2.17 TPSA 167.0 | ✓ Ro5 | ✓ Clean |
N[C@H](CC(=O)N[C@H](CC(=O)O)C(=O)O)C(=O)O
|
| ZINC1575288 | 0.560 | 248.2 Da LogP -2.17 TPSA 167.0 | ✓ Ro5 | ✓ Clean |
N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)O
|
| ZINC1575289 | 0.560 | 248.2 Da LogP -2.17 TPSA 167.0 | ✓ Ro5 | ✓ Clean |
N[C@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)O
|
| ZINC1575290 | 0.560 | 248.2 Da LogP -2.17 TPSA 167.0 | ✓ Ro5 | ✓ Clean |
N[C@@H](CC(=O)O)C(=O)N[C@H](CC(=O)O)C(=O)O
|
| ZINC1575291 | 0.560 | 248.2 Da LogP -2.17 TPSA 167.0 | ✓ Ro5 | ✓ Clean |
N[C@H](CC(=O)O)C(=O)N[C@H](CC(=O)O)C(=O)O
|
| ZINC5131760 | 0.560 | 237.2 Da LogP -0.94 TPSA 137.9 | ✓ Ro5 | ✓ Clean |
N[C@@H](CS[C@@H](CC(=O)O)C(=O)O)C(=O)O
|
| ZINC5131761 | 0.560 | 237.2 Da LogP -0.94 TPSA 137.9 | ✓ Ro5 | ✓ Clean |
N[C@H](CS[C@@H](CC(=O)O)C(=O)O)C(=O)O
|
| ZINC5131922 | 0.560 | 237.2 Da LogP -0.94 TPSA 137.9 | ✓ Ro5 | ✓ Clean |
N[C@@H](CS[C@H](CC(=O)O)C(=O)O)C(=O)O
|
| ZINC5131923 | 0.560 | 237.2 Da LogP -0.94 TPSA 137.9 | ✓ Ro5 | ✓ Clean |
N[C@H](CS[C@H](CC(=O)O)C(=O)O)C(=O)O
|
| ZINC2123927 | 0.538 | 204.2 Da LogP -1.62 TPSA 129.7 | ✓ Ro5 | ✓ Clean |
C[C@H](NC(=O)[C@@H](N)CC(=O)O)C(=O)O
|
| ZINC2560978 | 0.538 | 204.2 Da LogP -1.62 TPSA 129.7 | ✓ Ro5 | ✓ Clean |
C[C@H](NC(=O)C[C@H](N)C(=O)O)C(=O)O
|
| ZINC1730666 | 0.524 | 208.2 Da LogP -1.46 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@@H](CSC[C@H](N)C(=O)O)C(=O)O
|
| ZINC1730667 | 0.524 | 208.2 Da LogP -1.46 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@H](CSC[C@H](N)C(=O)O)C(=O)O
|
| ZINC1730669 | 0.524 | 208.2 Da LogP -1.46 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@H](CSC[C@@H](N)C(=O)O)C(=O)O
|
| ZINC3055005 | 0.524 | 204.2 Da LogP -0.63 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@@H](CCCC[C@H](N)C(=O)O)C(=O)O
|
| ZINC3055007 | 0.524 | 204.2 Da LogP -0.63 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@@H](CCCC[C@@H](N)C(=O)O)C(=O)O
|
| ZINC3055010 | 0.524 | 204.2 Da LogP -0.63 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@H](CCCC[C@@H](N)C(=O)O)C(=O)O
|
| ZINC100655912 | 0.519 | 478.4 Da LogP -4.25 TPSA 299.8 | 1 viol. | ✓ Clean |
N[C@H](CC(=O)O)C(=O)N[C@H](CC(=O)O)C(=O)N[C@H](…
|
| ZINC100655916 | 0.519 | 478.4 Da LogP -4.25 TPSA 299.8 | 1 viol. | ✓ Clean |
N[C@H](CC(=O)O)C(=O)N[C@H](CC(=O)O)C(=O)N[C@@H]…
|
| ZINC255993703 | 0.519 | 478.4 Da LogP -4.25 TPSA 299.8 | 1 viol. | ✓ Clean |
N[C@H](CC(=O)O)C(=O)N[C@H](CC(=O)O)C(=O)N[C@H](…
|
| ZINC4533843 | 0.519 | 363.3 Da LogP -3.21 TPSA 233.4 | 1 viol. | ✓ Clean |
N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@…
|
| ZINC4533848 | 0.519 | 478.4 Da LogP -4.25 TPSA 299.8 | 1 viol. | ✓ Clean |
N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@…
|
| ZINC4533853 | 0.519 | 478.4 Da LogP -4.25 TPSA 299.8 | 1 viol. | ✓ Clean |
N[C@H](CC(=O)O)C(=O)N[C@H](CC(=O)O)C(=O)N[C@@H]…
|
| ZINC1555366 | 0.500 | 232.3 Da LogP 0.15 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@@H](CCCCCC[C@H](N)C(=O)O)C(=O)O
|
| ZINC1555367 | 0.500 | 232.3 Da LogP 0.15 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@@H](CCCCCC[C@@H](N)C(=O)O)C(=O)O
|
| ZINC1555369 | 0.500 | 232.3 Da LogP 0.15 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@H](CCCCCC[C@@H](N)C(=O)O)C(=O)O
|
| ZINC1577651 | 0.500 | 234.2 Da LogP -0.66 TPSA 149.2 | ✓ Ro5 | ✓ Clean |
O=C(O)C[C@H](C(=O)O)[C@@H](CC(=O)O)C(=O)O
|
| ZINC1577652 | 0.500 | 234.2 Da LogP -0.66 TPSA 149.2 | ✓ Ro5 | ✓ Clean |
O=C(O)C[C@@H](C(=O)O)[C@@H](CC(=O)O)C(=O)O
|
| ZINC1577653 | 0.500 | 234.2 Da LogP -0.66 TPSA 149.2 | ✓ Ro5 | ✓ Clean |
O=C(O)C[C@H](C(=O)O)[C@H](CC(=O)O)C(=O)O
|
| ZINC1720127 | 0.500 | 218.3 Da LogP -0.24 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@@H](CCCCC[C@H](N)C(=O)O)C(=O)O
|
| ZINC1720128 | 0.500 | 218.3 Da LogP -0.24 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@@H](CCCCC[C@@H](N)C(=O)O)C(=O)O
|
| ZINC1720130 | 0.500 | 218.3 Da LogP -0.24 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@H](CCCCC[C@@H](N)C(=O)O)C(=O)O
|
| ZINC22923898 | 0.500 | 307.3 Da LogP -3.04 TPSA 199.3 | 1 viol. | ✓ Clean |
N[C@@H](CN[C@@H](CN[C@@H](CC(=O)O)C(=O)O)C(=O)O…
|
| ZINC22923905 | 0.500 | 307.3 Da LogP -3.04 TPSA 199.3 | 1 viol. | ✓ Clean |
N[C@@H](CN[C@H](CN[C@@H](CC(=O)O)C(=O)O)C(=O)O)…
|
| ZINC22930737 | 0.500 | 307.3 Da LogP -3.04 TPSA 199.3 | 1 viol. | ✓ Clean |
N[C@H](CN[C@H](CN[C@@H](CC(=O)O)C(=O)O)C(=O)O)C…
|
| ZINC23355305 | 0.500 | 307.3 Da LogP -3.04 TPSA 199.3 | 1 viol. | ✓ Clean |
N[C@H](CN[C@@H](CN[C@@H](CC(=O)O)C(=O)O)C(=O)O)…
|
| ZINC2384839 | 0.500 | 232.2 Da LogP -0.99 TPSA 129.7 | ✓ Ro5 | ✓ Clean |
CC(C)[C@H](NC(=O)[C@@H](N)CC(=O)O)C(=O)O
|
| ZINC2560328 | 0.500 | 239.1 Da LogP 1.53 TPSA 63.3 | ✓ Ro5 | ✓ Clean |
N[C@@H](CC(C(F)(F)F)C(F)(F)F)C(=O)O
|
| ZINC2560966 | 0.500 | 231.3 Da LogP -1.59 TPSA 135.5 | ✓ Ro5 | ✓ Clean |
CC(C)[C@H](NC(=O)[C@@H](N)CC(N)=O)C(=O)O
|
| ZINC3623257 | 0.500 | 202.2 Da LogP -0.85 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@@H](C/C=C/C[C@@H](N)C(=O)O)C(=O)O
|
| ZINC4348166 | 0.500 | 239.1 Da LogP 1.53 TPSA 63.3 | ✓ Ro5 | ✓ Clean |
N[C@H](CC(C(F)(F)F)C(F)(F)F)C(=O)O
|
| ZINC4580672 | 0.500 | 202.2 Da LogP -0.85 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@@H](C/C=C/C[C@H](N)C(=O)O)C(=O)O
|
| ZINC4580676 | 0.500 | 202.2 Da LogP -0.85 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@H](C/C=C/C[C@@H](N)C(=O)O)C(=O)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.