5DF8
CRYSTAL STRUCTURE OF PENICILLIN-BINDING PROTEIN 3 FROM PSEUDOMONAS AERUGINOSA IN COMPLEX WITH CEFOPERAZONE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000917 | biological_process | division septum assembly |
| A | 0004180 | molecular_function | carboxypeptidase activity |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006508 | biological_process | proteolysis |
| A | 0008360 | biological_process | regulation of cell shape |
| A | 0008658 | molecular_function | penicillin binding |
| A | 0008955 | molecular_function | peptidoglycan glycosyltransferase activity |
| A | 0009002 | molecular_function | serine-type D-Ala-D-Ala carboxypeptidase activity |
| A | 0009252 | biological_process | peptidoglycan biosynthetic process |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0043093 | biological_process | FtsZ-dependent cytokinesis |
| A | 0051301 | biological_process | cell division |
| A | 0071555 | biological_process | cell wall organization |
| B | 0000917 | biological_process | division septum assembly |
| B | 0004180 | molecular_function | carboxypeptidase activity |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006508 | biological_process | proteolysis |
| B | 0008360 | biological_process | regulation of cell shape |
| B | 0008658 | molecular_function | penicillin binding |
| B | 0008955 | molecular_function | peptidoglycan glycosyltransferase activity |
| B | 0009002 | molecular_function | serine-type D-Ala-D-Ala carboxypeptidase activity |
| B | 0009252 | biological_process | peptidoglycan biosynthetic process |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0043093 | biological_process | FtsZ-dependent cytokinesis |
| B | 0051301 | biological_process | cell division |
| B | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | binding site for residue 59F A 601 |
| Chain | Residue |
| A | SER294 |
| A | GLY486 |
| A | THR487 |
| A | ALA488 |
| A | ARG489 |
| A | TYR498 |
| A | TYR532 |
| A | HOH737 |
| A | HOH773 |
| A | HOH814 |
| A | HOH873 |
| A | TYR328 |
| A | VAL333 |
| A | SER349 |
| A | ASN351 |
| A | TYR407 |
| A | TYR409 |
| A | LYS484 |
| A | SER485 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 602 |
| Chain | Residue |
| A | GLY247 |
| A | SER248 |
| A | ARG284 |
| A | PHE290 |
| A | ASP525 |
| A | HOH766 |
| A | HOH837 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 603 |
| Chain | Residue |
| A | GLU176 |
| A | PRO278 |
| A | ARG282 |
| A | HOH832 |
| A | HOH870 |
| B | ARG473 |
| B | GOL603 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 604 |
| Chain | Residue |
| A | TYR268 |
| A | ASN269 |
| A | ASN272 |
| A | ARG273 |
| A | ASN275 |
| A | LEU276 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 605 |
| Chain | Residue |
| A | ARG387 |
| A | VAL388 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 606 |
| Chain | Residue |
| A | SER435 |
| A | MET436 |
| A | THR437 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 607 |
| Chain | Residue |
| A | VAL491 |
| A | ARG504 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 602 |
| Chain | Residue |
| B | GLY247 |
| B | SER248 |
| B | ARG284 |
| B | PHE290 |
| B | ARG504 |
| B | VAL523 |
| B | ASP525 |
| B | HOH754 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 603 |
| Chain | Residue |
| A | ARG282 |
| A | GOL603 |
| A | HOH870 |
| B | GLU234 |
| B | ALA238 |
| B | GLU241 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 604 |
| Chain | Residue |
| A | ARG473 |
| A | LEU536 |
| A | HOH716 |
| B | GLU176 |
| B | PRO278 |
| B | MET281 |
| B | ARG282 |
| B | HOH706 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 605 |
| Chain | Residue |
| B | HIS232 |
| B | ARG236 |
| B | GLN265 |
| B | THR267 |
| site_id | AD3 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 606 |
| Chain | Residue |
| B | VAL491 |
| B | ARG504 |
| site_id | AD4 |
| Number of Residues | 1 |
| Details | binding site for residue CL B 607 |
| Chain | Residue |
| B | ASN501 |
| site_id | AD5 |
| Number of Residues | 26 |
| Details | binding site for Di-peptide 59F B 601 and SER B 294 |
| Chain | Residue |
| B | HOH826 |
| B | HOH868 |
| B | PRO292 |
| B | GLY293 |
| B | THR295 |
| B | VAL296 |
| B | LYS297 |
| B | TYR328 |
| B | VAL333 |
| B | SER349 |
| B | ASN351 |
| B | TYR409 |
| B | LYS484 |
| B | SER485 |
| B | GLY486 |
| B | THR487 |
| B | ALA488 |
| B | ARG489 |
| B | TYR498 |
| B | TYR503 |
| B | TYR532 |
| B | PHE533 |
| B | GLY534 |
| B | HOH729 |
| B | HOH760 |
| B | HOH807 |
