3L76
Crystal Structure of Aspartate Kinase from Synechocystis
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 | 0009088 | biological_process | threonine biosynthetic process |
A | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
A | 0009090 | biological_process | homoserine biosynthetic process |
A | 0016301 | molecular_function | kinase 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 | 0009088 | biological_process | threonine biosynthetic process |
B | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
B | 0009090 | biological_process | homoserine biosynthetic process |
B | 0016301 | molecular_function | kinase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE THR A 601 |
Chain | Residue |
A | ASP280 |
A | HOH630 |
A | HOH631 |
A | ARG281 |
A | PRO282 |
A | GLY283 |
A | VAL284 |
A | ALA285 |
A | GLN304 |
A | ASN557 |
A | ILE558 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE THR A 602 |
Chain | Residue |
A | ASN385 |
A | ILE386 |
A | ASP454 |
A | ARG455 |
A | GLY457 |
A | MET458 |
A | ALA459 |
A | GLN478 |
A | HOH613 |
site_id | AC3 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE LYS A 603 |
Chain | Residue |
A | ASP298 |
A | ILE299 |
A | ASP300 |
A | MET537 |
A | HIS540 |
A | GLY542 |
A | VAL543 |
A | ALA544 |
A | THR563 |
A | SER564 |
A | ILE568 |
A | HOH614 |
A | HOH674 |
A | HOH691 |
site_id | AC4 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE LYS A 604 |
Chain | Residue |
A | MET365 |
A | ARG368 |
A | GLY370 |
A | ILE371 |
A | ALA372 |
A | SER392 |
A | GLU393 |
A | SER472 |
A | VAL473 |
A | ASP474 |
A | HOH607 |
A | HOH609 |
A | HOH624 |
A | HOH687 |
site_id | AC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SO4 A 605 |
Chain | Residue |
A | ARG277 |
A | ARG277 |
A | ASP308 |
A | ASP308 |
A | ASN310 |
A | ASN310 |
A | SER311 |
A | SER311 |
A | ARG483 |
A | ARG483 |
site_id | AC6 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE THR B 601 |
Chain | Residue |
B | ASN385 |
B | ILE386 |
B | VAL452 |
B | ASP454 |
B | ARG455 |
B | MET458 |
B | ALA459 |
B | GLN478 |
B | ILE493 |
B | HOH617 |
site_id | AC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE THR B 602 |
Chain | Residue |
B | ASP280 |
B | ARG281 |
B | PRO282 |
B | GLY283 |
B | VAL284 |
B | ALA285 |
B | GLN304 |
B | ASN557 |
B | ILE558 |
site_id | AC8 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE LYS B 603 |
Chain | Residue |
B | ASP298 |
B | ILE299 |
B | ASP300 |
B | MET537 |
B | HIS540 |
B | PRO541 |
B | GLY542 |
B | VAL543 |
B | ALA544 |
B | THR563 |
B | SER564 |
B | ILE568 |
B | HOH623 |
B | HOH649 |
site_id | AC9 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE LYS B 604 |
Chain | Residue |
B | SER472 |
B | VAL473 |
B | ASP474 |
B | HOH611 |
B | HOH651 |
B | MET365 |
B | ARG368 |
B | PRO369 |
B | GLY370 |
B | ILE371 |
B | ALA372 |
B | SER392 |
B | GLU393 |
Functional Information from PROSITE/UniProt
site_id | PS00324 |
Number of Residues | 9 |
Details | ASPARTOKINASE Aspartokinase signature. VqKFGGTSV |
Chain | Residue | Details |
A | VAL5-VAL13 |