5ZQD
Crystal Structure of Penicillin-Binding Protein D2 from Listeria monocytogenes in the Cefotaxime bound form
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006508 | biological_process | proteolysis |
| A | 0009002 | molecular_function | serine-type D-Ala-D-Ala carboxypeptidase activity |
| B | 0006508 | biological_process | proteolysis |
| B | 0009002 | molecular_function | serine-type D-Ala-D-Ala carboxypeptidase activity |
| C | 0006508 | biological_process | proteolysis |
| C | 0009002 | molecular_function | serine-type D-Ala-D-Ala carboxypeptidase activity |
| D | 0006508 | biological_process | proteolysis |
| D | 0009002 | molecular_function | serine-type D-Ala-D-Ala carboxypeptidase activity |
| E | 0006508 | biological_process | proteolysis |
| E | 0009002 | molecular_function | serine-type D-Ala-D-Ala carboxypeptidase activity |
| F | 0006508 | biological_process | proteolysis |
| F | 0009002 | molecular_function | serine-type D-Ala-D-Ala carboxypeptidase activity |
| G | 0006508 | biological_process | proteolysis |
| G | 0009002 | molecular_function | serine-type D-Ala-D-Ala carboxypeptidase activity |
| H | 0006508 | biological_process | proteolysis |
| H | 0009002 | molecular_function | serine-type D-Ala-D-Ala carboxypeptidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | binding site for residue CEF A 301 |
| Chain | Residue |
| A | ALA57 |
| A | ARG257 |
| A | HOH485 |
| A | SER58 |
| A | VAL94 |
| A | SER118 |
| A | ASN120 |
| A | THR223 |
| A | GLY224 |
| A | PHE225 |
| A | THR226 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue GOL A 302 |
| Chain | Residue |
| A | LEU69 |
| A | VAL72 |
| A | ASP73 |
| A | TRP79 |
| A | GLU187 |
| A | HOH427 |
| A | HOH467 |
| D | TYR28 |
| D | SER30 |
| D | LYS256 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 302 |
| Chain | Residue |
| B | VAL72 |
| B | ASP73 |
| B | TRP79 |
| B | GLU187 |
| B | HOH437 |
| C | TYR28 |
| C | SER30 |
| C | LYS256 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 303 |
| Chain | Residue |
| B | GLY164 |
| B | SER166 |
| B | GLU228 |
| B | HOH486 |
| F | GLY213 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue GOL B 304 |
| Chain | Residue |
| B | GLY42 |
| B | LYS172 |
| B | PHE175 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | binding site for residue GOL C 302 |
| Chain | Residue |
| B | TYR28 |
| B | LEU29 |
| B | SER30 |
| B | LYS256 |
| C | LEU69 |
| C | ASP73 |
| C | TRP79 |
| C | GLU187 |
| C | HOH457 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | binding site for residue GOL D 302 |
| Chain | Residue |
| A | TYR28 |
| A | SER30 |
| A | LYS256 |
| D | VAL72 |
| D | ASP73 |
| D | TRP79 |
| D | GLU187 |
| D | HOH461 |
| D | HOH482 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue GOL E 302 |
| Chain | Residue |
| E | VAL72 |
| E | ASP73 |
| E | TRP79 |
| E | GLU187 |
| E | HOH427 |
| H | SER30 |
| H | LYS256 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue GOL E 303 |
| Chain | Residue |
| E | SER30 |
| E | ASP250 |
| E | ALA251 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue GOL F 302 |
| Chain | Residue |
| F | VAL72 |
| F | ASP73 |
| F | TRP79 |
| F | GLU187 |
| F | HOH484 |
| G | SER30 |
| G | LYS256 |
| site_id | AD2 |
| Number of Residues | 9 |
| Details | binding site for residue GOL G 302 |
| Chain | Residue |
| F | TYR28 |
| F | SER30 |
| F | LYS256 |
| G | LEU69 |
| G | VAL72 |
| G | ASP73 |
| G | TRP79 |
| G | GLU187 |
| G | HOH416 |
| site_id | AD3 |
| Number of Residues | 9 |
| Details | binding site for residue GOL H 302 |
| Chain | Residue |
| E | TYR28 |
| E | LEU29 |
| E | HOH419 |
| H | LEU69 |
| H | VAL72 |
| H | ASP73 |
| H | TRP79 |
| H | GLU187 |
| H | HOH472 |
| site_id | AD4 |
| Number of Residues | 15 |
| Details | binding site for Di-peptide CEF B 301 and SER B 58 |
| Chain | Residue |
| B | LEU160 |
| B | THR223 |
| B | GLY224 |
| B | PHE225 |
| B | THR226 |
| B | ARG257 |
| B | ILE56 |
| B | ALA57 |
| B | LEU59 |
| B | SER60 |
| B | LYS61 |
| B | VAL94 |
| B | SER118 |
| B | ASN120 |
| B | SER158 |
| site_id | AD5 |
| Number of Residues | 16 |
| Details | binding site for Di-peptide CEF C 301 and SER C 58 |
| Chain | Residue |
| C | ILE56 |
| C | ALA57 |
| C | LEU59 |
| C | SER60 |
| C | LYS61 |
| C | SER118 |
| C | ASN120 |
| C | SER158 |
| C | LEU160 |
| C | LYS222 |
| C | THR223 |
| C | GLY224 |
| C | PHE225 |
| C | THR226 |
| C | ARG257 |
| C | HOH405 |
| site_id | AD6 |
| Number of Residues | 16 |
| Details | binding site for Di-peptide CEF C 303 and LYS C 204 |
| Chain | Residue |
| A | LYS82 |
| A | LEU83 |
| A | ASP84 |
| A | THR104 |
| A | HOH409 |
| C | VAL197 |
| C | THR198 |
| C | GLY202 |
| C | ALA203 |
| C | LEU205 |
| C | HOH401 |
| C | HOH412 |
| C | HOH422 |
| C | HOH483 |
| C | HOH488 |
| C | HOH502 |
| site_id | AD7 |
| Number of Residues | 20 |
| Details | binding site for Di-peptide CEF D 301 and SER D 58 |
| Chain | Residue |
| D | ILE56 |
| D | ALA57 |
| D | LEU59 |
| D | SER60 |
| D | LYS61 |
| D | VAL94 |
| D | SER118 |
| D | ASN120 |
| D | SER158 |
| D | LEU160 |
| D | THR208 |
| D | LYS222 |
| D | THR223 |
| D | GLY224 |
| D | PHE225 |
| D | THR226 |
| D | ARG257 |
| D | HOH401 |
| D | HOH444 |
| D | HOH491 |
| site_id | AD8 |
| Number of Residues | 13 |
| Details | binding site for Di-peptide CEF D 303 and LYS D 204 |
| Chain | Residue |
| B | LYS82 |
| B | LEU83 |
| B | ASP84 |
| B | THR104 |
| B | HOH406 |
| B | HOH422 |
| D | VAL197 |
| D | GLY202 |
| D | ALA203 |
| D | LEU205 |
| D | HOH405 |
| D | HOH438 |
| D | HOH450 |
| site_id | AD9 |
| Number of Residues | 17 |
| Details | binding site for Di-peptide CEF E 301 and SER E 58 |
| Chain | Residue |
| E | ILE56 |
| E | ALA57 |
| E | LEU59 |
| E | SER60 |
| E | LYS61 |
| E | VAL94 |
| E | SER118 |
| E | ASN120 |
| E | SER158 |
| E | LEU160 |
| E | THR208 |
| E | THR223 |
| E | GLY224 |
| E | PHE225 |
| E | THR226 |
| E | ARG257 |
| E | HOH405 |
| site_id | AE1 |
| Number of Residues | 17 |
| Details | binding site for Di-peptide CEF F 301 and SER F 58 |
| Chain | Residue |
| F | ILE56 |
| F | ALA57 |
| F | LEU59 |
| F | SER60 |
| F | LYS61 |
| F | VAL94 |
| F | SER118 |
| F | ASN120 |
| F | SER158 |
| F | LEU160 |
| F | LYS222 |
| F | THR223 |
| F | GLY224 |
| F | PHE225 |
| F | THR226 |
| F | ARG257 |
| F | HOH454 |
| site_id | AE2 |
| Number of Residues | 18 |
| Details | binding site for Di-peptide CEF G 301 and SER G 58 |
| Chain | Residue |
| G | ILE56 |
| G | ALA57 |
| G | LEU59 |
| G | SER60 |
| G | LYS61 |
| G | VAL94 |
| G | SER118 |
| G | ASN120 |
| G | SER158 |
| G | LEU160 |
| G | LYS222 |
| G | THR223 |
| G | GLY224 |
| G | PHE225 |
| G | THR226 |
| G | ARG257 |
| G | HOH458 |
| G | HOH498 |
| site_id | AE3 |
| Number of Residues | 8 |
| Details | binding site for Di-peptide CEF G 303 and LYS G 204 |
| Chain | Residue |
| G | VAL197 |
| G | GLY202 |
| G | ALA203 |
| G | LEU205 |
| G | GLU206 |
| G | HOH401 |
| G | HOH403 |
| G | HOH470 |
| site_id | AE4 |
| Number of Residues | 16 |
| Details | binding site for Di-peptide CEF H 301 and SER H 58 |
| Chain | Residue |
| H | ILE56 |
| H | ALA57 |
| H | LEU59 |
| H | SER60 |
| H | LYS61 |
| H | VAL94 |
| H | SER118 |
| H | ASN120 |
| H | SER158 |
| H | THR208 |
| H | THR223 |
| H | GLY224 |
| H | PHE225 |
| H | THR226 |
| H | ARG257 |
| H | HOH491 |
| site_id | AE5 |
| Number of Residues | 8 |
| Details | binding site for Di-peptide CEF H 303 and LYS H 204 |
| Chain | Residue |
| H | VAL197 |
| H | GLY202 |
| H | ALA203 |
| H | LEU205 |
| H | GLU206 |
| H | HOH438 |
| H | HOH446 |
| H | HOH520 |






