Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008658 | molecular_function | penicillin binding |
A | 0008800 | molecular_function | beta-lactamase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0017001 | biological_process | antibiotic catabolic process |
A | 0046677 | biological_process | response to antibiotic |
B | 0008658 | molecular_function | penicillin binding |
B | 0008800 | molecular_function | beta-lactamase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0017001 | biological_process | antibiotic catabolic process |
B | 0046677 | biological_process | response to antibiotic |
C | 0008658 | molecular_function | penicillin binding |
C | 0008800 | molecular_function | beta-lactamase activity |
C | 0016787 | molecular_function | hydrolase activity |
C | 0017001 | biological_process | antibiotic catabolic process |
C | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE TLA A 267 |
Chain | Residue |
A | SER72 |
B | ARG242 |
A | LYS75 |
A | ASN119 |
A | SER120 |
A | LYS210 |
A | THR211 |
A | GLY212 |
A | TRP213 |
A | ARG249 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE EDO A 268 |
Chain | Residue |
A | MET117 |
A | ARG118 |
A | LEU196 |
A | ILE198 |
A | THR199 |
A | ALA209 |
A | LYS210 |
A | HOH286 |
A | HOH379 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 269 |
Chain | Residue |
A | GLU62 |
A | ALA65 |
A | HOH415 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE TLA B 267 |
Chain | Residue |
B | SER72 |
B | LYS75 |
B | SER120 |
B | LYS210 |
B | THR211 |
B | ARG249 |
B | HOH276 |
B | HOH279 |
B | HOH346 |
site_id | AC5 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE P6G B 268 |
Chain | Residue |
A | LEU38 |
A | GLN39 |
A | PHE247 |
B | TRP97 |
B | PHE104 |
B | ALA105 |
B | SER120 |
B | THR121 |
B | VAL122 |
B | TRP123 |
B | GLU126 |
B | LEU127 |
B | HOH356 |
B | HOH393 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO B 269 |
Chain | Residue |
B | ALA65 |
B | SER167 |
B | HIS169 |
B | EDO272 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO B 270 |
Chain | Residue |
B | MET117 |
B | ARG118 |
B | LEU196 |
B | THR199 |
B | ALA209 |
B | HOH331 |
B | HOH361 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO B 271 |
Chain | Residue |
B | VAL94 |
B | ASP112 |
B | HOH273 |
C | PRO227 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO B 272 |
Chain | Residue |
B | ALA65 |
B | ARG67 |
B | EDO269 |
Functional Information from PROSITE/UniProt
site_id | PS00337 |
Number of Residues | 11 |
Details | BETA_LACTAMASE_D Beta-lactamase class-D active site. PaSTFKIPhTL |
Chain | Residue | Details |
C | PRO70-LEU80 | |
A | PRO70-LEU80 | |
B | PRO70-LEU80 | |