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 | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 601 |
| Chain | Residue |
| B | ASP253 |
| B | ASP351 |
| B | LYS443 |
| B | IOT603 |
| B | POP604 |
| B | HOH615 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 602 |
| Chain | Residue |
| B | HOH765 |
| B | HOH766 |
| B | HOH767 |
| B | GLU280 |
| B | IOT603 |
| B | POP604 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 603 |
| Chain | Residue |
| A | ASP253 |
| A | ASP351 |
| A | LYS443 |
| A | POP605 |
| A | IOT606 |
| A | HOH734 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 604 |
| Chain | Residue |
| A | LEU444 |
| A | POP605 |
| A | IOT606 |
| A | HOH608 |
| A | HOH788 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE POP A 605 |
| Chain | Residue |
| A | SER249 |
| A | GLY251 |
| A | ASP253 |
| A | SER254 |
| A | ASP351 |
| A | LYS423 |
| A | LYS443 |
| A | LEU444 |
| A | MG603 |
| A | MG604 |
| A | IOT606 |
| A | HOH608 |
| A | HOH623 |
| A | HOH788 |
| site_id | AC6 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE IOT A 606 |
| Chain | Residue |
| A | VAL247 |
| A | LEU248 |
| A | SER249 |
| A | SER254 |
| A | SER272 |
| A | MET273 |
| A | TYR326 |
| A | LEU330 |
| A | LEU333 |
| A | GLY347 |
| A | TYR348 |
| A | GLY349 |
| A | ASP351 |
| A | ILE352 |
| A | MET357 |
| A | ASP373 |
| A | GLU382 |
| A | LYS443 |
| A | LEU444 |
| A | GLY445 |
| A | VAL446 |
| A | MG603 |
| A | MG604 |
| A | POP605 |
| A | HOH608 |
| A | HOH646 |
| A | HOH734 |
| site_id | AC7 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE IOT B 603 |
| Chain | Residue |
| B | VAL247 |
| B | LEU248 |
| B | SER254 |
| B | VAL271 |
| B | MET273 |
| B | TYR326 |
| B | LEU333 |
| B | GLY347 |
| B | TYR348 |
| B | GLY349 |
| B | ASP351 |
| B | ILE352 |
| B | MET357 |
| B | ASP373 |
| B | LEU380 |
| B | GLU382 |
| B | LYS443 |
| B | MG601 |
| B | MG602 |
| B | POP604 |
| B | HOH615 |
| B | HOH638 |
| site_id | AC8 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE POP B 604 |
| Chain | Residue |
| B | SER249 |
| B | GLY251 |
| B | ASP253 |
| B | SER254 |
| B | ASP351 |
| B | LYS423 |
| B | LYS443 |
| B | MG601 |
| B | MG602 |
| B | IOT603 |
| B | HOH614 |
| B | HOH615 |
| B | HOH767 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL A 607 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL B 605 |
| Chain | Residue |
| B | SER278 |
| B | PRO329 |
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 |
