2J0X
CRYSTAL STRUCTURE OF E. COLI ASPARTOKINASE III IN COMPLEX WITH LYSINE AND ASPARTATE (T-STATE)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004072 | molecular_function | aspartate kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009085 | biological_process | lysine biosynthetic process |
| A | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
| A | 0009090 | biological_process | homoserine biosynthetic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004072 | molecular_function | aspartate kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009085 | biological_process | lysine biosynthetic process |
| B | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
| B | 0009090 | biological_process | homoserine biosynthetic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 A1000 |
| Chain | Residue |
| B | LYS8 |
| B | GLY10 |
| B | GLY11 |
| B | SER39 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ASP A 502 |
| Chain | Residue |
| A | SER201 |
| A | ASP202 |
| A | HOH2051 |
| A | SER39 |
| A | PHE184 |
| A | ARG198 |
| A | GLY199 |
| A | GLY200 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE LYS A1451 |
| Chain | Residue |
| A | MET318 |
| A | SER321 |
| A | GLY323 |
| A | PHE324 |
| A | LEU325 |
| A | SER345 |
| A | GLU346 |
| A | HOH2039 |
| B | SER338 |
| B | VAL339 |
| B | ASP340 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE LYS B1450 |
| Chain | Residue |
| A | SER338 |
| A | VAL339 |
| A | ASP340 |
| B | MET318 |
| B | SER321 |
| B | GLY323 |
| B | PHE324 |
| B | LEU325 |
| B | SER345 |
Functional Information from PROSITE/UniProt
| site_id | PS00324 |
| Number of Residues | 9 |
| Details | ASPARTOKINASE Aspartokinase signature. VsKFGGTSV |
| Chain | Residue | Details |
| A | VAL6-VAL14 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 81 |
| Details | Domain: {"description":"ACT","evidences":[{"source":"PROSITE-ProRule","id":"PRU01007","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 203 |
| Details | Region: {"description":"Interface"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 150 |
| Details | Region: {"description":"Required for homodimerization"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 24 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"2J0X","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 243 |
| Details | Region: {"description":"Aspartokinase"} |
| Chain | Residue | Details |
