1ZQ1
Structure of GatDE tRNA-Dependent Amidotransferase from Pyrococcus abyssi
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004067 | molecular_function | asparaginase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0006412 | biological_process | translation |
A | 0006450 | biological_process | regulation of translational fidelity |
A | 0006520 | biological_process | amino acid metabolic process |
A | 0016874 | molecular_function | ligase activity |
A | 0050567 | molecular_function | glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity |
B | 0004067 | molecular_function | asparaginase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005524 | molecular_function | ATP binding |
B | 0006412 | biological_process | translation |
B | 0006450 | biological_process | regulation of translational fidelity |
B | 0006520 | biological_process | amino acid metabolic process |
B | 0016874 | molecular_function | ligase activity |
B | 0050567 | molecular_function | glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity |
C | 0003824 | molecular_function | catalytic activity |
C | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
C | 0005515 | molecular_function | protein binding |
C | 0005524 | molecular_function | ATP binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0006412 | biological_process | translation |
C | 0016874 | molecular_function | ligase activity |
C | 0016884 | molecular_function | carbon-nitrogen ligase activity, with glutamine as amido-N-donor |
C | 0050567 | molecular_function | glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity |
D | 0003824 | molecular_function | catalytic activity |
D | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
D | 0005515 | molecular_function | protein binding |
D | 0005524 | molecular_function | ATP binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0006412 | biological_process | translation |
D | 0016874 | molecular_function | ligase activity |
D | 0016884 | molecular_function | carbon-nitrogen ligase activity, with glutamine as amido-N-donor |
D | 0050567 | molecular_function | glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ASP A 1000 |
Chain | Residue |
A | PHE145 |
A | SER146 |
A | GLU147 |
A | THR178 |
A | ASP179 |
A | ALA204 |
B | TYR376 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ASP B 5000 |
Chain | Residue |
B | GLU147 |
B | THR178 |
B | ASP179 |
B | GLN205 |
A | TYR376 |
B | SER146 |
Functional Information from PROSITE/UniProt
site_id | PS00144 |
Number of Residues | 9 |
Details | ASN_GLN_ASE_1 Asparaginase / glutaminase active site signature 1. IiGTGGTIA |
Chain | Residue | Details |
A | ILE96-ALA104 |
site_id | PS00917 |
Number of Residues | 11 |
Details | ASN_GLN_ASE_2 Asparaginase / glutaminase active site signature 2. GvVvaHGTDTM |
Chain | Residue | Details |
A | GLY171-MSE181 |
site_id | PS01234 |
Number of Residues | 15 |
Details | GATB Glutamyl-tRNA(Gln) amidotransferase subunit B signature. LDRlgiPLIEIsTtP |
Chain | Residue | Details |
C | LEU180-PRO194 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00586 |
Chain | Residue | Details |
A | THR102 | |
A | THR178 | |
A | ASP179 | |
A | LYS256 | |
B | THR102 | |
B | THR178 | |
B | ASP179 | |
B | LYS256 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 3eca |
Chain | Residue | Details |
A | THR102 | |
A | ASP179 | |
A | THR178 | |
A | TYR115 | |
A | LYS256 |
site_id | CSA2 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 3eca |
Chain | Residue | Details |
B | THR102 | |
B | ASP179 | |
B | THR178 | |
B | TYR115 | |
B | LYS256 |
site_id | CSA3 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 3eca |
Chain | Residue | Details |
A | THR102 | |
A | THR178 | |
A | TYR115 | |
B | SER377 |
site_id | CSA4 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 3eca |
Chain | Residue | Details |
A | SER377 | |
B | THR102 | |
B | TYR115 | |
B | THR178 |
site_id | CSA5 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 3eca |
Chain | Residue | Details |
A | GLY379 |
site_id | CSA6 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 3eca |
Chain | Residue | Details |
B | GLY379 |