4USJ
N-acetylglutamate kinase from Arabidopsis thaliana in complex with PII from Chlamydomonas reinhardtii
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003991 | molecular_function | acetylglutamate kinase activity |
| 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 |
| B | 0003991 | molecular_function | acetylglutamate kinase activity |
| 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 |
| C | 0006808 | biological_process | regulation of nitrogen utilization |
| C | 0030234 | molecular_function | enzyme regulator activity |
| D | 0006808 | biological_process | regulation of nitrogen utilization |
| D | 0030234 | molecular_function | enzyme regulator activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ARG A 301 |
| Chain | Residue |
| A | LYS210 |
| A | LYS232 |
| A | GLU284 |
| A | ILE285 |
| A | SER287 |
| A | ASP288 |
| A | GLU289 |
| A | GLY292 |
| A | MET294 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ADP A 302 |
| Chain | Residue |
| A | LYS41 |
| A | GLY43 |
| A | GLY44 |
| A | ALA45 |
| A | THR215 |
| A | ASP216 |
| A | GLY219 |
| A | LEU221 |
| A | LYS247 |
| A | ALA249 |
| A | GLY251 |
| A | MET252 |
| A | LYS255 |
| A | MG304 |
| A | HOH2006 |
| A | HOH2007 |
| A | HOH2031 |
| B | GLN152 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE NLG A 303 |
| Chain | Residue |
| A | GLY75 |
| A | GLY76 |
| A | GLY77 |
| A | LEU97 |
| A | ARG98 |
| A | ASN192 |
| A | ASN194 |
| A | ALA195 |
| A | HOH2005 |
| A | HOH2007 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 304 |
| Chain | Residue |
| A | ADP302 |
| A | HOH2005 |
| A | HOH2007 |
| A | HOH2031 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ARG B 301 |
| Chain | Residue |
| B | PHE33 |
| B | LYS210 |
| B | LYS232 |
| B | GLU284 |
| B | ILE285 |
| B | SER287 |
| B | ASP288 |
| B | GLU289 |
| B | GLY290 |
| B | GLY292 |
| B | MET294 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE X2W B 303 |
| Chain | Residue |
| B | LYS41 |
| B | GLY44 |
| B | GLY75 |
| B | GLY76 |
| B | GLY77 |
| B | LEU97 |
| B | ARG98 |
| B | ASN192 |
| B | ASN194 |
| B | ALA195 |
| B | HOH2028 |
| B | HOH2029 |
| B | HOH2030 |
| site_id | AC7 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE ATP C 301 |
| Chain | Residue |
| C | ILE24 |
| C | GLY44 |
| C | LEU45 |
| C | THR46 |
| C | GLY52 |
| C | VAL53 |
| C | GLY54 |
| C | GLN56 |
| C | ASP80 |
| C | VAL82 |
| C | ILE104 |
| C | GLY105 |
| C | ASP106 |
| C | GLY107 |
| C | LYS108 |
| C | PHE110 |
| C | ARG119 |
| C | ARG121 |
| C | MET132 |
| C | MG302 |
| C | GLN303 |
| C | HOH2008 |
| C | HOH2009 |
| C | HOH2010 |
| C | HOH2018 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG C 302 |
| Chain | Residue |
| C | GLY54 |
| C | ATP301 |
| C | HOH2009 |
| C | HOH2010 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GLN C 303 |
| Chain | Residue |
| C | GLU130 |
| C | MET132 |
| C | MET136 |
| C | GLU137 |
| C | ATP301 |
| C | ILE42 |
| C | ARG43 |
| C | GLY44 |
| C | VAL82 |
| C | GLN87 |
| site_id | BC1 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE ATP D 301 |
| Chain | Residue |
| D | ILE24 |
| D | GLY44 |
| D | LEU45 |
| D | THR46 |
| D | GLY52 |
| D | VAL53 |
| D | GLY54 |
| D | GLN56 |
| D | ASP80 |
| D | VAL82 |
| D | ILE104 |
| D | GLY105 |
| D | ASP106 |
| D | GLY107 |
| D | LYS108 |
| D | ARG119 |
| D | ARG121 |
| D | MET132 |
| D | MG302 |
| D | GLN303 |
| D | HOH2012 |
| D | HOH2013 |
| D | HOH2017 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG D 302 |
| Chain | Residue |
| D | GLY54 |
| D | ATP301 |
| D | HOH2012 |
| D | HOH2013 |
| site_id | BC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GLN D 303 |
| Chain | Residue |
| D | ILE42 |
| D | ARG43 |
| D | GLY44 |
| D | VAL82 |
| D | GLN87 |
| D | GLU130 |
| D | MET132 |
| D | GLY135 |
| D | MET136 |
| D | GLU137 |
| D | ATP301 |
Functional Information from PROSITE/UniProt
| site_id | PS00638 |
| Number of Residues | 14 |
| Details | PII_GLNB_CTER P-II protein C-terminal region signature. TgeiGDGKIFVhpV |
| Chain | Residue | Details |
| C | THR101-VAL114 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25416954","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4USJ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 22 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17913711","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25416954","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2RD5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4USJ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17913711","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2RD5","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
