3NG0
Crystal Structure of Glutamine Synthetase from Synechocystis sp. PCC 6803
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 | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006542 | biological_process | glutamine biosynthetic process |
| 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 | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ANP A 474 |
| Chain | Residue |
| A | TYR128 |
| A | ARG342 |
| A | ARG347 |
| A | LYS356 |
| A | ARG359 |
| A | GLU361 |
| A | MN475 |
| A | MN476 |
| A | MN477 |
| A | GLU132 |
| A | GLU210 |
| A | LYS211 |
| A | ILE226 |
| A | LYS227 |
| A | PHE228 |
| A | HIS274 |
| A | SER276 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN A 475 |
| Chain | Residue |
| A | GLU134 |
| A | GLU215 |
| A | GLU223 |
| A | ANP474 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MN A 476 |
| Chain | Residue |
| A | GLU132 |
| A | ANP474 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 477 |
| Chain | Residue |
| A | GLU132 |
| A | HIS272 |
| A | GLU361 |
| A | ARG363 |
| A | ANP474 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 85 |
| Details | Domain: {"description":"GS beta-grasp","evidences":[{"source":"PROSITE-ProRule","id":"PRU01330","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"JUN-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of glutamine synthetase from Synechocystis sp. PCC 6803.","authors":["Saelices L.","Cascio D.","Florencio F.J.","Muro-Pastor M.I."]}},{"source":"PDB","id":"3NG0","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of glutamine synthetase from Synechocystis sp. PCC 6803.","authors":["Saelices L.","Cascio D.","Florencio F.J.","Muro-Pastor M.I."]}},{"source":"PDB","id":"3NG0","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P9WN39","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P12425","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P0A1P6","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
