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 | ASP232 | |
A | GLU235 | |
A | GLY236 | |
B | ASP232 | |
B | GLU235 | |
B | GLY236 | |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | TYR318 | |
A | SER331 | |
A | ASN356 | |
B | TYR318 | |
B | SER331 | |
B | ASN356 | |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | SITE: Binds to carbapenem drug (covalent) |
Chain | Residue | Details |
A | CYS354 | |
B | CYS354 | |