8V1Y
Composite map of AMPylated GlnA bound to hinT
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004356 | molecular_function | glutamine synthetase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006541 | biological_process | glutamine metabolic process |
| A | 0006542 | biological_process | glutamine biosynthetic process |
| A | 0009314 | biological_process | response to radiation |
| A | 0016020 | cellular_component | membrane |
| A | 0016874 | molecular_function | ligase activity |
| A | 0019676 | biological_process | ammonia assimilation cycle |
| A | 0019740 | biological_process | nitrogen utilization |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004356 | molecular_function | glutamine synthetase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006541 | biological_process | glutamine metabolic process |
| B | 0006542 | biological_process | glutamine biosynthetic process |
| B | 0009314 | biological_process | response to radiation |
| B | 0016020 | cellular_component | membrane |
| B | 0016874 | molecular_function | ligase activity |
| B | 0019676 | biological_process | ammonia assimilation cycle |
| B | 0019740 | biological_process | nitrogen utilization |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0043530 | molecular_function | adenosine 5'-monophosphoramidase activity |
| C | 0055130 | biological_process | D-alanine catabolic process |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0043530 | molecular_function | adenosine 5'-monophosphoramidase activity |
| D | 0055130 | biological_process | D-alanine catabolic process |
Functional Information from PROSITE/UniProt
| site_id | PS00180 |
| Number of Residues | 19 |
| Details | GLNA_1 Glutamine synthetase signature 1. FDGSSiggwkginESDmvL |
| Chain | Residue | Details |
| A | PHE50-LEU68 |
| site_id | PS00181 |
| Number of Residues | 16 |
| Details | GLNA_ATP Glutamine synthetase putative ATP-binding region signature. KPMfgd..NGSGmHchmS |
| Chain | Residue | Details |
| A | LYS259-SER274 |
| site_id | PS00182 |
| Number of Residues | 13 |
| Details | GLNA_ADENYLATION Glutamine synthetase class-I adenylation site. KIhpgeaMDKNLY |
| Chain | Residue | Details |
| A | LYS386-TYR398 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P9WN39","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P0A1P6","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P12425","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P77961","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"O-AMP-tyrosine","evidences":[{"source":"PubMed","id":"4904088","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"5543675","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 84 |
| Details | Domain: {"description":"GS beta-grasp","evidences":[{"source":"PROSITE-ProRule","id":"PRU01330","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 12 |
| Details | Motif: {"description":"Histidine triad motif","evidences":[{"source":"PubMed","id":"20934431","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Tele-AMP-histidine intermediate","evidences":[{"source":"PubMed","id":"15703176","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20934431","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20934431","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3N1S","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
