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 | 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 | 0042803 | molecular_function | protein homodimerization 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 | 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 | 16 |
Details | BINDING: |
Chain | Residue | Details |
A | LYS8 | |
B | THR45 | |
B | GLU119 | |
B | ARG198 | |
B | THR221 | |
B | TYR227 | |
B | ARG232 | |
B | LYS257 | |
A | THR45 | |
A | GLU119 | |
A | ARG198 | |
A | THR221 | |
A | TYR227 | |
A | ARG232 | |
A | LYS257 | |
B | LYS8 |
site_id | SWS_FT_FI2 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0007744|PDB:2J0X |
Chain | Residue | Details |
A | MET318 | |
B | SER345 | |
A | SER321 | |
A | PHE324 | |
A | SER338 | |
A | SER345 | |
B | MET318 | |
B | SER321 | |
B | PHE324 | |
B | SER338 |