6XG1
Class C beta-lactamase from Escherichia coli
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008800 | molecular_function | beta-lactamase activity |
| A | 0017001 | biological_process | antibiotic catabolic process |
| A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| B | 0008800 | molecular_function | beta-lactamase activity |
| B | 0017001 | biological_process | antibiotic catabolic process |
| B | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 401 |
| Chain | Residue |
| A | PHE68 |
| A | THR69 |
| A | TRP70 |
| A | HOH508 |
| A | HOH513 |
| A | HOH680 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 402 |
| Chain | Residue |
| A | HOH511 |
| A | HOH516 |
| A | HOH527 |
| A | HOH836 |
| A | GLY143 |
| A | PRO145 |
| A | LEU176 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue EDO A 403 |
| Chain | Residue |
| A | GLN83 |
| A | GLN84 |
| A | HIS213 |
| A | THR253 |
| A | GLU255 |
| A | ASP256 |
| A | HOH514 |
| A | HOH698 |
| A | HOH718 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 404 |
| Chain | Residue |
| A | LEU281 |
| A | SER284 |
| A | TYR286 |
| A | PRO331 |
| A | HOH535 |
| A | HOH773 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 501 |
| Chain | Residue |
| B | GLU223 |
| B | HIS237 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 502 |
| Chain | Residue |
| B | ILE311 |
| B | PRO374 |
| B | ALA375 |
| B | HOH606 |
| B | HOH608 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 503 |
| Chain | Residue |
| B | GLY108 |
| B | LYS111 |
| B | ASP114 |
| B | LYS118 |
| B | TYR119 |
Functional Information from PROSITE/UniProt
| site_id | PS00336 |
| Number of Residues | 8 |
| Details | BETA_LACTAMASE_C Beta-lactamase class-C active site. FELGSVSK |
| Chain | Residue | Details |
| A | PHE87-LYS94 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Acyl-ester intermediate => ECO:0000255|PROSITE-ProRule:PRU10102, ECO:0000269|PubMed:11478888, ECO:0000269|PubMed:12005439, ECO:0000269|PubMed:16506777, ECO:0000269|PubMed:35486701, ECO:0000269|PubMed:6795623, ECO:0000269|PubMed:9819201, ECO:0000269|DOI:10.1021/ja001676x |
| Chain | Residue | Details |
| A | SER91 | |
| B | SER91 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16506777, ECO:0000269|DOI:10.1021/ja001676x, ECO:0007744|PDB:1FCN, ECO:0007744|PDB:2FFY |
| Chain | Residue | Details |
| A | SER91 | |
| B | SER91 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12005439, ECO:0000269|PubMed:12323371, ECO:0007744|PDB:1KVM, ECO:0007744|PDB:1LL9 |
| Chain | Residue | Details |
| A | GLN147 | |
| B | GLN147 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16506777, ECO:0007744|PDB:2FFY |
| Chain | Residue | Details |
| A | TYR177 | |
| B | TYR177 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12005439, ECO:0000269|PubMed:12323371, ECO:0000269|PubMed:16506777, ECO:0000269|DOI:10.1021/ja001676x, ECO:0007744|PDB:1FCN, ECO:0007744|PDB:1KVM, ECO:0007744|PDB:1LL9, ECO:0007744|PDB:2FFY |
| Chain | Residue | Details |
| A | ASN179 | |
| A | ALA345 | |
| B | ASN179 | |
| B | ALA345 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12005439, ECO:0007744|PDB:1KVM |
| Chain | Residue | Details |
| A | ASN370 | |
| B | ASN370 |
