2JJ4
The complex of PII and acetylglutamate kinase from Synechococcus elongatus PCC7942
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003991 | molecular_function | acetylglutamate kinase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006526 | biological_process | L-arginine biosynthetic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0042802 | molecular_function | identical protein binding |
| B | 0003991 | molecular_function | acetylglutamate kinase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006526 | biological_process | L-arginine biosynthetic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0042802 | molecular_function | identical protein binding |
| C | 0003991 | molecular_function | acetylglutamate kinase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006526 | biological_process | L-arginine biosynthetic process |
| C | 0016301 | molecular_function | kinase activity |
| C | 0042802 | molecular_function | identical protein binding |
| D | 0005515 | molecular_function | protein binding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005829 | cellular_component | cytosol |
| D | 0006808 | biological_process | regulation of nitrogen utilization |
| D | 0030234 | molecular_function | enzyme regulator activity |
| D | 0042802 | molecular_function | identical protein binding |
| E | 0005515 | molecular_function | protein binding |
| E | 0005524 | molecular_function | ATP binding |
| E | 0005829 | cellular_component | cytosol |
| E | 0006808 | biological_process | regulation of nitrogen utilization |
| E | 0030234 | molecular_function | enzyme regulator activity |
| E | 0042802 | molecular_function | identical protein binding |
| F | 0005515 | molecular_function | protein binding |
| F | 0005524 | molecular_function | ATP binding |
| F | 0005829 | cellular_component | cytosol |
| F | 0006808 | biological_process | regulation of nitrogen utilization |
| F | 0030234 | molecular_function | enzyme regulator activity |
| F | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE NLG A 1292 |
| Chain | Residue |
| A | GLY69 |
| A | GLY70 |
| A | GLY71 |
| A | ILE74 |
| A | LEU91 |
| A | ARG92 |
| A | SER174 |
| A | ASN185 |
| A | ALA188 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE NLG B 1292 |
| Chain | Residue |
| B | GLY69 |
| B | GLY70 |
| B | GLY71 |
| B | ILE74 |
| B | GLY90 |
| B | LEU91 |
| B | ARG92 |
| B | ASN185 |
| B | ALA188 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00082","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_00082","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"7592328","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"O-UMP-tyrosine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00675","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1oh9 |
| Chain | Residue | Details |
| A | GLY38 | |
| A | LYS35 | |
| A | LYS248 | |
| A | GLY71 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1oh9 |
| Chain | Residue | Details |
| B | GLY38 | |
| B | LYS35 | |
| B | LYS248 | |
| B | GLY71 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1oh9 |
| Chain | Residue | Details |
| C | GLY38 | |
| C | LYS35 | |
| C | LYS248 | |
| C | GLY71 |
