3QHY
Structural, thermodynamic and kinetic analysis of the picomolar binding affinity interaction of the beta-lactamase inhibitor protein-II (BLIP-II) with class A beta-lactamases
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008800 | molecular_function | beta-lactamase activity |
| A | 0017001 | biological_process | antibiotic catabolic process |
| A | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
| A | 0046677 | biological_process | response to antibiotic |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0061630 | molecular_function | ubiquitin protein ligase activity |
Functional Information from PROSITE/UniProt
| site_id | PS00146 |
| Number of Residues | 16 |
| Details | BETA_LACTAMASE_A Beta-lactamase class-A active site. FaFASTyKalaAGVLL |
| Chain | Residue | Details |
| A | PHE66-LEU81 |
| site_id | PS00626 |
| Number of Residues | 11 |
| Details | RCC1_2 Regulator of chromosome condensation (RCC1) signature 2. IAGGyFHGLAL |
| Chain | Residue | Details |
| B | ILE69-LEU79 | |
| B | ILE108-LEU118 | |
| B | VAL225-LEU235 |






