3PBK
Structural and Functional Studies of Fatty Acyl-Adenylate Ligases from E. coli and L. pneumophila
Replaces: 3GQWFunctional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005886 | cellular_component | plasma membrane |
A | 0006633 | biological_process | fatty acid biosynthetic process |
A | 0008610 | biological_process | lipid biosynthetic process |
A | 0016877 | molecular_function | ligase activity, forming carbon-sulfur bonds |
A | 0070566 | molecular_function | adenylyltransferase activity |
B | 0005886 | cellular_component | plasma membrane |
B | 0006633 | biological_process | fatty acid biosynthetic process |
B | 0008610 | biological_process | lipid biosynthetic process |
B | 0016877 | molecular_function | ligase activity, forming carbon-sulfur bonds |
B | 0070566 | molecular_function | adenylyltransferase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE 1ZZ A 1 |
Chain | Residue |
A | ILE208 |
A | LEU339 |
A | ALA340 |
A | LEU344 |
A | ASP445 |
A | VAL456 |
A | ARG459 |
A | SER549 |
A | LYS551 |
A | ASP230 |
A | GLY235 |
A | ALA308 |
A | GLU309 |
A | PRO310 |
A | CYS336 |
A | TYR337 |
A | GLY338 |
site_id | AC2 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE 1ZZ B 585 |
Chain | Residue |
B | ILE208 |
B | GLY235 |
B | ALA308 |
B | GLU309 |
B | PRO310 |
B | ILE311 |
B | CYS336 |
B | TYR337 |
B | GLY338 |
B | LEU339 |
B | ALA340 |
B | LEU344 |
B | ASP445 |
B | VAL456 |
B | ARG459 |
B | SER549 |
B | LYS551 |
B | HOH609 |