5DF7
CRYSTAL STRUCTURE OF PENICILLIN-BINDING PROTEIN 3 FROM PSEUDOMONAS AERUGINOSA IN COMPLEX WITH AZLOCILLIN
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 | 16 |
Details | binding site for residue 59H A 601 |
Chain | Residue |
A | SER294 |
A | ARG489 |
A | TYR498 |
A | PHE533 |
A | GLY534 |
A | HOH716 |
A | HOH726 |
A | HOH841 |
A | TYR328 |
A | SER349 |
A | ASN351 |
A | TYR409 |
A | SER485 |
A | GLY486 |
A | THR487 |
A | ALA488 |
site_id | AC2 |
Number of Residues | 9 |
Details | binding site for residue GOL A 602 |
Chain | Residue |
A | GLY247 |
A | SER248 |
A | ARG284 |
A | PHE290 |
A | ARG504 |
A | VAL523 |
A | ASP525 |
A | HOH731 |
A | HOH757 |
site_id | AC3 |
Number of Residues | 2 |
Details | binding site for residue CL A 603 |
Chain | Residue |
A | ARG499 |
A | ASN501 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue IMD A 604 |
Chain | Residue |
A | ALA181 |
A | PHE182 |
A | LEU381 |
site_id | AC5 |
Number of Residues | 8 |
Details | binding site for residue GOL B 602 |
Chain | Residue |
B | GLY247 |
B | SER248 |
B | ARG284 |
B | PHE290 |
B | ALA415 |
B | VAL523 |
B | ASP525 |
B | HOH701 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue GOL B 603 |
Chain | Residue |
B | TYR268 |
B | ASN269 |
B | ASN272 |
B | ARG273 |
B | HOH716 |
site_id | AC7 |
Number of Residues | 2 |
Details | binding site for residue CL B 604 |
Chain | Residue |
A | ARG175 |
B | ARG473 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue CL B 605 |
Chain | Residue |
B | LYS490 |
B | VAL491 |
B | ARG504 |
site_id | AC9 |
Number of Residues | 3 |
Details | binding site for residue CL B 606 |
Chain | Residue |
A | ARG473 |
B | ARG175 |
B | HOH802 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue IMD B 607 |
Chain | Residue |
B | ALA181 |
B | PHE182 |
B | LEU381 |
B | HOH792 |
site_id | AD2 |
Number of Residues | 23 |
Details | binding site for Di-peptide 59H B 601 and SER B 294 |
Chain | Residue |
B | PRO292 |
B | GLY293 |
B | THR295 |
B | VAL296 |
B | LYS297 |
B | TYR328 |
B | VAL333 |
B | SER349 |
B | ASN351 |
B | TYR407 |
B | TYR409 |
B | LYS484 |
B | SER485 |
B | GLY486 |
B | THR487 |
B | ALA488 |
B | ARG489 |
B | TYR498 |
B | PHE533 |
B | GLY534 |
B | HOH712 |
B | HOH714 |
B | HOH818 |