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 602 |
| Chain | Residue |
| B | SER249 |
| B | POP704 |
| B | AMP705 |
| B | HOH842 |
| B | HOH843 |
| B | HOH844 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 605 |
| Chain | Residue |
| B | AMP705 |
| B | HOH727 |
| B | ASP253 |
| B | ASP351 |
| B | POP704 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 601 |
| Chain | Residue |
| A | ASP253 |
| A | ASP351 |
| A | LYS443 |
| A | POP701 |
| A | AMP702 |
| A | HOH812 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 603 |
| Chain | Residue |
| A | LEU444 |
| A | POP701 |
| A | AMP702 |
| A | HOH813 |
| A | HOH814 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE POP A 701 |
| Chain | Residue |
| A | SER249 |
| A | GLY251 |
| A | ILE252 |
| A | ASP253 |
| A | SER254 |
| A | ASP351 |
| A | LYS423 |
| A | LYS443 |
| A | LEU444 |
| A | MG601 |
| A | MG603 |
| A | AMP702 |
| A | HOH726 |
| A | HOH814 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PCX B 706 |
| Chain | Residue |
| B | TYR326 |
| B | TYR348 |
| B | GLY349 |
| B | ASP351 |
| B | ILE352 |
| B | MET357 |
| B | ASP373 |
| B | LEU380 |
| B | GLU382 |
| B | LYS443 |
| B | AMP705 |
| B | HOH724 |
| B | HOH727 |
| B | HOH855 |
| site_id | AC7 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE AMP A 702 |
| Chain | Residue |
| A | VAL247 |
| A | LEU248 |
| A | SER249 |
| A | SER254 |
| A | VAL271 |
| A | SER272 |
| A | MET273 |
| A | LEU330 |
| A | LEU333 |
| A | THR346 |
| A | GLY347 |
| A | TYR348 |
| A | ASP351 |
| A | LYS443 |
| A | LEU444 |
| A | VAL446 |
| A | MG601 |
| A | MG603 |
| A | POP701 |
| A | PCX703 |
| A | HOH812 |
| A | HOH813 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PCX A 703 |
| Chain | Residue |
| A | TYR326 |
| A | TYR348 |
| A | GLY349 |
| A | ASP351 |
| A | ILE352 |
| A | ASP373 |
| A | LEU380 |
| A | GLU382 |
| A | LYS443 |
| A | AMP702 |
| A | HOH710 |
| A | HOH812 |
| site_id | AC9 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE AMP B 705 |
| Chain | Residue |
| B | VAL247 |
| B | LEU248 |
| B | SER254 |
| B | VAL271 |
| B | MET273 |
| B | LEU330 |
| B | GLY347 |
| B | TYR348 |
| B | ASP351 |
| B | MG602 |
| B | MG605 |
| B | POP704 |
| B | PCX706 |
| B | HOH727 |
| B | HOH931 |
| site_id | BC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE POP B 704 |
| Chain | Residue |
| B | SER249 |
| B | GLY251 |
| B | ASP253 |
| B | SER254 |
| B | ASP351 |
| B | LYS423 |
| B | LYS443 |
| B | MG602 |
| B | MG605 |
| B | AMP705 |
| B | HOH727 |
| B | HOH749 |
| B | HOH843 |
| B | HOH864 |
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 |
