Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004066 | molecular_function | asparagine synthase (glutamine-hydrolyzing) activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005829 | cellular_component | cytosol |
| 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 | 0000166 | molecular_function | nucleotide binding |
| B | 0004066 | molecular_function | asparagine synthase (glutamine-hydrolyzing) activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005829 | cellular_component | cytosol |
| 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 901 |
| Chain | Residue |
| B | ASP253 |
| B | ASP351 |
| B | APC802 |
| B | HOH986 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 902 |
| Chain | Residue |
| A | ASP253 |
| A | ASP351 |
| A | LYS443 |
| A | APC801 |
| A | HOH922 |
| site_id | AC3 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE APC A 801 |
| Chain | Residue |
| A | VAL247 |
| A | LEU248 |
| A | SER249 |
| A | GLY251 |
| A | ILE252 |
| A | ASP253 |
| A | SER254 |
| A | VAL271 |
| A | SER272 |
| A | MET273 |
| A | LEU330 |
| A | GLY347 |
| A | TYR348 |
| A | ASP351 |
| A | LYS423 |
| A | LYS443 |
| A | CMA803 |
| A | MG902 |
| A | HOH922 |
| A | HOH1086 |
| A | HOH1148 |
| A | HOH1151 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE CMA A 803 |
| Chain | Residue |
| A | TYR326 |
| A | TYR348 |
| A | GLY349 |
| A | ASP351 |
| A | ILE352 |
| A | ASP373 |
| A | GLU382 |
| A | APC801 |
| A | HOH922 |
| A | HOH938 |
| A | HOH955 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE APC B 802 |
| Chain | Residue |
| B | VAL247 |
| B | LEU248 |
| B | SER249 |
| B | GLY251 |
| B | ILE252 |
| B | ASP253 |
| B | SER254 |
| B | VAL271 |
| B | SER272 |
| B | MET273 |
| B | LEU330 |
| B | LEU333 |
| B | GLY347 |
| B | TYR348 |
| B | ASP351 |
| B | LYS423 |
| B | LYS443 |
| B | CMA804 |
| B | MG901 |
| B | HOH960 |
| B | HOH1101 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CMA B 804 |
| Chain | Residue |
| B | TYR326 |
| B | TYR348 |
| B | GLY349 |
| B | ASP351 |
| B | ILE352 |
| B | MET357 |
| B | ASP373 |
| B | GLU382 |
| B | LYS443 |
| B | APC802 |
| B | HOH986 |
| B | HOH1045 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 709 |
| Chain | Residue |
| B | LEU245 |
| B | THR270 |
| B | ARG294 |
| B | ARG342 |
| B | HOH922 |
| B | HOH948 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 710 |
| Chain | Residue |
| B | LEU13 |
| B | SER15 |
| B | ALA48 |
| B | THR49 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL B 711 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 712 |
| Chain | Residue |
| A | ASP406 |
| A | HOH918 |
| A | HOH1079 |
| B | SER213 |
| B | ARG215 |
| B | GOL713 |
| B | HOH1058 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 713 |
| Chain | Residue |
| B | ARG215 |
| B | LEU217 |
| B | SER410 |
| B | GOL712 |
| B | HOH930 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {} |
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 |
1JGT
