1Q19
Carbapenam Synthetase
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 | 0017000 | biological_process | antibiotic biosynthetic process |
| 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 | 0017000 | biological_process | antibiotic biosynthetic process |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004066 | molecular_function | asparagine synthase (glutamine-hydrolyzing) activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005829 | cellular_component | cytosol |
| C | 0016874 | molecular_function | ligase activity |
| C | 0017000 | biological_process | antibiotic biosynthetic process |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004066 | molecular_function | asparagine synthase (glutamine-hydrolyzing) activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005829 | cellular_component | cytosol |
| D | 0016874 | molecular_function | ligase activity |
| D | 0017000 | biological_process | antibiotic biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 504 |
| Chain | Residue |
| A | ILE444 |
| A | APC505 |
| A | HOH507 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG D 504 |
| Chain | Residue |
| D | SER246 |
| D | ILE444 |
| D | APC505 |
| D | HOH553 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 504 |
| Chain | Residue |
| B | APC505 |
| B | HOH548 |
| B | SER246 |
| B | ILE444 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG C 504 |
| Chain | Residue |
| C | SER246 |
| C | ILE444 |
| C | APC505 |
| site_id | AC5 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE APC A 505 |
| Chain | Residue |
| A | PRO244 |
| A | LEU245 |
| A | SER246 |
| A | GLY248 |
| A | LEU249 |
| A | ASP250 |
| A | SER251 |
| A | TYR268 |
| A | SER269 |
| A | ILE270 |
| A | LEU327 |
| A | THR343 |
| A | GLY344 |
| A | TYR345 |
| A | ASP348 |
| A | LYS421 |
| A | LYS443 |
| A | ILE444 |
| A | GLY445 |
| A | ILE446 |
| A | MG504 |
| A | SSC506 |
| A | HOH507 |
| A | HOH560 |
| A | HOH598 |
| site_id | AC6 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE APC B 505 |
| Chain | Residue |
| B | PRO244 |
| B | LEU245 |
| B | SER246 |
| B | GLY248 |
| B | LEU249 |
| B | ASP250 |
| B | SER251 |
| B | TYR268 |
| B | SER269 |
| B | ILE270 |
| B | LEU327 |
| B | GLY344 |
| B | TYR345 |
| B | ASP348 |
| B | LYS421 |
| B | LYS443 |
| B | ILE444 |
| B | GLY445 |
| B | ILE446 |
| B | MG504 |
| B | SSC506 |
| B | HOH507 |
| B | HOH554 |
| site_id | AC7 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE APC C 505 |
| Chain | Residue |
| C | PRO244 |
| C | LEU245 |
| C | SER246 |
| C | GLY248 |
| C | LEU249 |
| C | ASP250 |
| C | SER251 |
| C | TYR268 |
| C | SER269 |
| C | ILE270 |
| C | THR343 |
| C | GLY344 |
| C | TYR345 |
| C | ASP348 |
| C | LYS421 |
| C | LYS442 |
| C | ILE444 |
| C | GLY445 |
| C | ILE446 |
| C | SER450 |
| C | MG504 |
| C | SSC506 |
| site_id | AC8 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE APC D 505 |
| Chain | Residue |
| D | LYS443 |
| D | ILE444 |
| D | GLY445 |
| D | ILE446 |
| D | MG504 |
| D | SSC506 |
| D | HOH529 |
| D | HOH554 |
| D | HOH565 |
| D | PRO244 |
| D | LEU245 |
| D | SER246 |
| D | GLY248 |
| D | LEU249 |
| D | ASP250 |
| D | SER251 |
| D | TYR268 |
| D | SER269 |
| D | ILE270 |
| D | LEU327 |
| D | THR343 |
| D | GLY344 |
| D | ASP348 |
| D | LYS421 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SSC A 506 |
| Chain | Residue |
| A | ILE323 |
| A | TYR345 |
| A | GLY346 |
| A | LEU349 |
| A | ARG374 |
| A | GLU380 |
| A | APC505 |
| A | HOH561 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SSC B 506 |
| Chain | Residue |
| B | ILE323 |
| B | TYR345 |
| B | GLY346 |
| B | ASP348 |
| B | LEU349 |
| B | GLN371 |
| B | APC505 |
| B | HOH543 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SSC D 506 |
| Chain | Residue |
| D | LEU319 |
| D | ILE323 |
| D | TYR345 |
| D | GLY346 |
| D | ASP348 |
| D | GLN371 |
| D | APC505 |
| D | HOH554 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SSC C 506 |
| Chain | Residue |
| C | LEU319 |
| C | TYR345 |
| C | GLY346 |
| C | GLN371 |
| C | ARG374 |
| C | APC505 |
| C | HOH527 |
| C | HOH543 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 860 |
| Details | Domain: {"description":"Asparagine synthetase"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"19371088","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"19371088","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 72 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12890666","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
