3E2K
Crystal Structure of the KPC-2 Beta-lactamase/Beta-lactamase inhibitor protein (BLIP)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008800 | molecular_function | beta-lactamase activity |
| A | 0016787 | molecular_function | hydrolase 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 | 0008800 | molecular_function | beta-lactamase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0017001 | biological_process | antibiotic catabolic process |
| B | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
| B | 0046677 | biological_process | response to antibiotic |
| C | 0005515 | molecular_function | protein binding |
| C | 0005576 | cellular_component | extracellular region |
| C | 0033252 | biological_process | regulation of beta-lactamase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005576 | cellular_component | extracellular region |
| D | 0033252 | biological_process | regulation of beta-lactamase activity |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile; acyl-ester intermediate => ECO:0000269|PubMed:33257320, ECO:0007744|PDB:6Z23, ECO:0007744|PDB:6Z24 |
| Chain | Residue | Details |
| A | SER70 | |
| B | SER70 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250 |
| Chain | Residue | Details |
| A | GLU168 | |
| B | GLU168 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:28388065, ECO:0000269|PubMed:33257320, ECO:0007744|PDB:5UJ3, ECO:0007744|PDB:6Z23, ECO:0007744|PDB:6Z24 |
| Chain | Residue | Details |
| A | SER70 | |
| A | THR237 | |
| B | SER70 | |
| B | THR237 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:28388065, ECO:0007744|PDB:5UJ3 |
| Chain | Residue | Details |
| A | LYS73 | |
| B | LYS73 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:33257320, ECO:0000312|PDB:6Z24 |
| Chain | Residue | Details |
| A | TRP105 | |
| B | TRP105 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:28388065, ECO:0000269|PubMed:33257320, ECO:0007744|PDB:5UJ3, ECO:0007744|PDB:6Z23 |
| Chain | Residue | Details |
| A | SER130 | |
| B | SER130 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:33257320, ECO:0007744|PDB:6Z23, ECO:0007744|PDB:6Z24 |
| Chain | Residue | Details |
| A | ASN132 | |
| B | ASN132 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:28388065, ECO:0007744|PDB:5UJ3, ECO:0007744|PDB:6Z24 |
| Chain | Residue | Details |
| A | THR235 | |
| B | THR235 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1btl |
| Chain | Residue | Details |
| A | GLU166 | |
| A | LYS73 | |
| A | SER130 | |
| A | SER70 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1btl |
| Chain | Residue | Details |
| B | GLU166 | |
| B | LYS73 | |
| B | SER130 | |
| B | SER70 |
