Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004066 | molecular_function | asparagine synthase (glutamine-hydrolyzing) activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005829 | cellular_component | cytosol |
A | 0006529 | biological_process | asparagine biosynthetic process |
A | 0016874 | molecular_function | ligase activity |
A | 0033050 | biological_process | clavulanic acid biosynthetic process |
A | 0034027 | molecular_function | (carboxyethyl)arginine beta-lactam-synthase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0004066 | molecular_function | asparagine synthase (glutamine-hydrolyzing) activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005829 | cellular_component | cytosol |
B | 0006529 | biological_process | asparagine biosynthetic process |
B | 0016874 | molecular_function | ligase activity |
B | 0033050 | biological_process | clavulanic acid biosynthetic process |
B | 0034027 | molecular_function | (carboxyethyl)arginine beta-lactam-synthase activity |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG B 601 |
Chain | Residue |
B | ASP253 |
B | ASP351 |
B | ATP702 |
B | HOH946 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 602 |
Chain | Residue |
B | SER249 |
B | ATP702 |
B | HOH792 |
B | HOH793 |
B | HOH903 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG A 603 |
Chain | Residue |
A | ATP701 |
A | POP705 |
A | HOH801 |
A | HOH884 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 604 |
Chain | Residue |
A | ASP253 |
A | ASP351 |
A | ATP701 |
A | POP705 |
A | AMP706 |
A | HOH885 |
site_id | AC5 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE ATP B 702 |
Chain | Residue |
B | VAL247 |
B | LEU248 |
B | SER249 |
B | ASP253 |
B | SER254 |
B | VAL271 |
B | SER272 |
B | MET273 |
B | LEU330 |
B | THR346 |
B | GLY347 |
B | TYR348 |
B | ASP351 |
B | LYS423 |
B | LYS443 |
B | MG601 |
B | MG602 |
B | HOH792 |
B | HOH903 |
B | HOH904 |
B | HOH946 |
site_id | AC6 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE POP A 705 |
Chain | Residue |
A | SER249 |
A | GLY251 |
A | ASP253 |
A | SER254 |
A | ASP351 |
A | LYS423 |
A | LYS443 |
A | MG603 |
A | MG604 |
A | AMP706 |
A | HOH773 |
A | HOH885 |
site_id | AC7 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE AMP A 706 |
Chain | Residue |
A | VAL247 |
A | LEU248 |
A | SER254 |
A | VAL271 |
A | SER272 |
A | MET273 |
A | TYR326 |
A | LEU330 |
A | GLY347 |
A | TYR348 |
A | MG604 |
A | POP705 |
A | HOH885 |
site_id | AC8 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE ATP A 701 |
Chain | Residue |
A | VAL247 |
A | LEU248 |
A | SER249 |
A | GLY251 |
A | ILE252 |
A | ASP253 |
A | SER254 |
A | VAL271 |
A | MET273 |
A | LEU330 |
A | GLY347 |
A | TYR348 |
A | ASP351 |
A | LYS423 |
A | LYS443 |
A | MG603 |
A | MG604 |
A | HOH773 |
A | HOH801 |
A | HOH884 |
A | HOH885 |
A | HOH886 |
A | HOH897 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP253 | |
A | ASP351 | |
B | ASP253 | |
B | ASP351 | |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 303 |
Chain | Residue | Details |
A | TYR348 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | GLU382 | electrostatic stabiliser, hydrogen bond donor, increase acidity, increase basicity |
A | LYS443 | electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA2 |
Number of Residues | 3 |
Details | M-CSA 303 |
Chain | Residue | Details |
B | TYR348 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | GLU382 | electrostatic stabiliser, hydrogen bond donor, increase acidity, increase basicity |
B | LYS443 | electrostatic stabiliser, hydrogen bond donor |