5KDR
The crystal structure of carboxyltransferase from Staphylococcus Aureus bound to the antimicrobial agent moiramide B.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006633 | biological_process | fatty acid biosynthetic process |
| A | 0009317 | cellular_component | acetyl-CoA carboxylase complex |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016743 | molecular_function | carboxyl- or carbamoyltransferase activity |
| A | 0016874 | molecular_function | ligase activity |
| A | 2001295 | biological_process | malonyl-CoA biosynthetic process |
| B | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006633 | biological_process | fatty acid biosynthetic process |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0009317 | cellular_component | acetyl-CoA carboxylase complex |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016743 | molecular_function | carboxyl- or carbamoyltransferase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 2001295 | biological_process | malonyl-CoA biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 401 |
| Chain | Residue |
| A | LYS185 |
| A | ARG295 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 402 |
| Chain | Residue |
| A | ARG89 |
| A | ALA164 |
| A | ARG168 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | binding site for residue YT5 B 301 |
| Chain | Residue |
| B | GLY167 |
| B | ALA168 |
| B | THR206 |
| B | GLY207 |
| B | GLY208 |
| B | ALA231 |
| B | GLY232 |
| B | VAL235 |
| A | SER198 |
| A | LEU229 |
| B | MET134 |
| B | GLY166 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 302 |
| Chain | Residue |
| A | HIS83 |
| B | LYS262 |
| B | HOH407 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 303 |
| Chain | Residue |
| B | HIS58 |
| B | HIS203 |
| B | GLU223 |
| B | PRO224 |
| B | ALA226 |
| B | ARG266 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 304 |
| Chain | Residue |
| B | CYS33 |
| B | CYS36 |
| B | CYS52 |
| B | CYS55 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 22 |
| Details | ZN_FING: C4-type => ECO:0000255|HAMAP-Rule:MF_01395 |
| Chain | Residue | Details |
| B | CYS33-CYS55 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01395 |
| Chain | Residue | Details |
| B | CYS33 | |
| B | CYS36 | |
| B | CYS52 | |
| B | CYS55 |
