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 |
A | 0046872 | molecular_function | metal ion binding |
A | 0071555 | biological_process | cell wall organization |
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 |
B | 0046872 | molecular_function | metal ion binding |
B | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | binding site for residue 5VR A 301 |
Chain | Residue |
A | ALA69 |
A | ARG214 |
A | ARG250 |
A | HOH511 |
A | HOH517 |
A | SER70 |
A | SER118 |
A | VAL120 |
A | LYS208 |
A | THR209 |
A | GLY210 |
A | TYR211 |
A | THR213 |
site_id | AC2 |
Number of Residues | 2 |
Details | binding site for residue CL A 302 |
Chain | Residue |
A | ARG206 |
B | ARG206 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue CD A 303 |
Chain | Residue |
A | ASP143 |
A | HOH448 |
A | HOH606 |
B | ASP143 |
B | HOH488 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue CD A 304 |
Chain | Residue |
A | GLU37 |
A | HIS38 |
A | GLU125 |
A | GLU256 |
A | CO307 |
A | HOH572 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue CO A 305 |
Chain | Residue |
A | GLU147 |
A | CO306 |
A | HOH438 |
B | HIS140 |
B | GLU147 |
B | HOH436 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue CO A 306 |
Chain | Residue |
A | HIS140 |
A | GLU147 |
A | CO305 |
A | HOH438 |
B | GLU147 |
B | HOH436 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue CO A 307 |
Chain | Residue |
A | HIS34 |
A | GLU37 |
A | GLU256 |
A | CD304 |
A | HOH572 |
A | HOH613 |
site_id | AC8 |
Number of Residues | 2 |
Details | binding site for residue CO B 301 |
Chain | Residue |
B | HIS140 |
B | HOH527 |
site_id | AC9 |
Number of Residues | 3 |
Details | binding site for residue CO B 302 |
Chain | Residue |
A | HIS140 |
A | HOH581 |
A | HOH611 |
site_id | AD1 |
Number of Residues | 3 |
Details | binding site for residue CO B 303 |
Chain | Residue |
B | HIS34 |
B | GLU37 |
B | GLU256 |
site_id | AD2 |
Number of Residues | 3 |
Details | binding site for residue CO B 305 |
Chain | Residue |
A | HIS178 |
A | HOH648 |
B | HIS90 |
Functional Information from PROSITE/UniProt
site_id | PS00337 |
Number of Residues | 11 |
Details | BETA_LACTAMASE_D Beta-lactamase class-D active site. PaSTFKIPnSL |
Chain | Residue | Details |
A | PRO68-LEU78 | |