7VQN
Crystal structure of KPC-2 beta-lactamase complexed with hydrolyzed EXW-1
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 | 0008800 | molecular_function | beta-lactamase activity |
C | 0016787 | molecular_function | hydrolase activity |
C | 0017001 | biological_process | antibiotic catabolic process |
C | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
C | 0046677 | biological_process | response to antibiotic |
D | 0008800 | molecular_function | beta-lactamase activity |
D | 0016787 | molecular_function | hydrolase activity |
D | 0017001 | biological_process | antibiotic catabolic process |
D | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
D | 0046677 | biological_process | response to antibiotic |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Nucleophile; acyl-ester intermediate => ECO:0000269|PubMed:33257320, ECO:0007744|PDB:6Z23, ECO:0007744|PDB:6Z24 |
Chain | Residue | Details |
A | SER69 | |
B | SER69 | |
C | SER69 | |
D | SER69 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor => ECO:0000250 |
Chain | Residue | Details |
A | GLU167 | |
B | GLU167 | |
C | GLU167 | |
D | GLU167 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
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 | SER69 | |
A | THR236 | |
B | SER69 | |
B | THR236 | |
C | SER69 | |
C | THR236 | |
D | SER69 | |
D | THR236 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:28388065, ECO:0007744|PDB:5UJ3 |
Chain | Residue | Details |
A | LYS72 | |
B | LYS72 | |
C | LYS72 | |
D | LYS72 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:33257320, ECO:0000312|PDB:6Z24 |
Chain | Residue | Details |
A | TRP104 | |
B | TRP104 | |
C | TRP104 | |
D | TRP104 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:28388065, ECO:0000269|PubMed:33257320, ECO:0007744|PDB:5UJ3, ECO:0007744|PDB:6Z23 |
Chain | Residue | Details |
A | SER129 | |
B | SER129 | |
C | SER129 | |
D | SER129 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:33257320, ECO:0007744|PDB:6Z23, ECO:0007744|PDB:6Z24 |
Chain | Residue | Details |
A | ASN131 | |
B | ASN131 | |
C | ASN131 | |
D | ASN131 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:28388065, ECO:0007744|PDB:5UJ3, ECO:0007744|PDB:6Z24 |
Chain | Residue | Details |
A | THR234 | |
B | THR234 | |
C | THR234 | |
D | THR234 |