Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0008360 | biological_process | regulation of cell shape |
| A | 0009252 | biological_process | peptidoglycan biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0018104 | biological_process | peptidoglycan-protein cross-linking |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0071555 | biological_process | cell wall organization |
| A | 0071972 | molecular_function | peptidoglycan L,D-transpeptidase activity |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0008360 | biological_process | regulation of cell shape |
| B | 0009252 | biological_process | peptidoglycan biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016746 | molecular_function | acyltransferase activity |
| B | 0018104 | biological_process | peptidoglycan-protein cross-linking |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0071555 | biological_process | cell wall organization |
| B | 0071972 | molecular_function | peptidoglycan L,D-transpeptidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | binding site for residue NO3 A 501 |
| Chain | Residue |
| A | ASP108 |
| A | ARG111 |
| A | HOH637 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue TRS A 502 |
| Chain | Residue |
| A | ASP160 |
| A | GLY161 |
| A | HOH848 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 503 |
| Chain | Residue |
| A | HIS214 |
| A | PHE215 |
| A | HOH869 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 504 |
| Chain | Residue |
| A | SER306 |
| A | PRO311 |
| A | HOH602 |
| A | HOH861 |
| B | ASN95 |
| B | ASN97 |
| B | ARG99 |
| B | ARG122 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 505 |
| Chain | Residue |
| A | HOH601 |
| A | HOH773 |
| B | SER65 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 506 |
| Chain | Residue |
| A | VAL75 |
| A | ALA77 |
| A | PRO78 |
| A | GLN117 |
| A | LEU118 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | binding site for residue EDO A 507 |
| Chain | Residue |
| A | ASN95 |
| A | ASN97 |
| A | ARG99 |
| A | ARG122 |
| A | HOH603 |
| A | HOH904 |
| B | SER306 |
| B | GLY309 |
| B | PRO311 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 508 |
| Chain | Residue |
| A | ASN95 |
| A | VAL101 |
| A | GLU116 |
| A | GLY119 |
| A | ARG122 |
| A | TYR124 |
| A | HOH607 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 509 |
| Chain | Residue |
| A | GLN140 |
| A | TRP364 |
| A | HIS368 |
| A | HOH622 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 510 |
| Chain | Residue |
| A | SER65 |
| A | THR74 |
| A | ALA77 |
| A | PRO78 |
| A | VAL79 |
| A | HOH754 |
| A | HOH832 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue NA A 511 |
| Chain | Residue |
| A | ILE188 |
| A | LYS189 |
| A | ILE190 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue NA A 512 |
| Chain | Residue |
| A | GLY250 |
| A | ASP251 |
| A | LYS370 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 513 |
| Chain | Residue |
| A | TYR318 |
| A | THR320 |
| A | HIS352 |
| A | HOH761 |
| A | HOH851 |
| site_id | AD5 |
| Number of Residues | 10 |
| Details | binding site for residue EDO A 514 |
| Chain | Residue |
| A | TYR318 |
| A | SER331 |
| A | GLY332 |
| A | HIS352 |
| A | GLY353 |
| A | HOH613 |
| A | HOH619 |
| A | HOH627 |
| A | HOH728 |
| A | HOH903 |
| site_id | AD6 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 515 |
| Chain | Residue |
| A | TYR201 |
| A | GLY387 |
| A | ILE388 |
| A | HOH732 |
| A | HOH876 |
| site_id | AD7 |
| Number of Residues | 3 |
| Details | binding site for residue NO3 B 501 |
| Chain | Residue |
| B | ASP108 |
| B | ARG111 |
| B | HOH737 |
| site_id | AD8 |
| Number of Residues | 6 |
| Details | binding site for residue TRS B 502 |
| Chain | Residue |
| B | GLU213 |
| B | HIS214 |
| B | PHE215 |
| B | ILE291 |
| B | TRP394 |
| B | HOH812 |
| site_id | AD9 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 503 |
| Chain | Residue |
| B | VAL75 |
| B | ALA77 |
| B | PRO78 |
| B | GLN117 |
| B | LEU118 |
| B | HOH776 |
| site_id | AE1 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 504 |
| Chain | Residue |
| B | SER65 |
| B | THR74 |
| B | ALA77 |
| B | PRO78 |
| B | HOH784 |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | HIS336 | |
| B | HIS336 | |
| Chain | Residue | Details |
| A | CYS354 | |
| B | CYS354 | |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLY236 | |
| B | ASP232 | |
| B | GLU235 | |
| B | GLY236 | |
| A | ASP232 | |
| A | GLU235 | |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| B | SER331 | |
| B | ASN356 | |
| A | TYR318 | |
| A | SER331 | |
| A | ASN356 | |
| B | TYR318 | |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | SITE: Binds to carbapenem drug (covalent) |
| Chain | Residue | Details |
| A | CYS354 | |
| B | CYS354 | |
