6WHF
class C beta-lactamase from Escherichia coli in complex with cephalothin
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 | 8 |
| Details | binding site for residue EDO A 501 |
| Chain | Residue |
| A | GLU299 |
| A | SER314 |
| A | HIS341 |
| A | LYS342 |
| A | THR343 |
| A | HOH629 |
| A | HOH632 |
| A | HOH642 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 502 |
| Chain | Residue |
| A | EDO503 |
| A | HOH620 |
| A | THR69 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 503 |
| Chain | Residue |
| A | PHE68 |
| A | THR69 |
| A | EDO502 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 504 |
| Chain | Residue |
| A | LYS153 |
| A | PRO240 |
| A | GLY241 |
| A | ALA242 |
| A | HOH686 |
| A | HOH715 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 505 |
| Chain | Residue |
| A | ARG107 |
| A | THR203 |
| A | GLU272 |
| A | HOH639 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | binding site for residue 9EP A 506 |
| Chain | Residue |
| A | SER91 |
| A | GLN147 |
| A | ASN179 |
| A | TYR248 |
| A | ASN316 |
| A | GLY344 |
| A | ALA345 |
| A | THR346 |
| A | GLY347 |
| A | ASN370 |
| A | HOH704 |
| A | HOH723 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | binding site for residue EDO B 501 |
| Chain | Residue |
| B | HIS237 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 502 |
| Chain | Residue |
| B | GLU299 |
| B | HIS341 |
| B | LYS342 |
| B | THR343 |
| B | HOH626 |
| B | HOH641 |
| B | HOH644 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 503 |
| Chain | Residue |
| B | ILE311 |
| B | PRO374 |
| B | ALA375 |
| B | HOH744 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 504 |
| Chain | Residue |
| B | GLY108 |
| B | GLU109 |
| B | ILE110 |
| B | LYS111 |
| B | ASP114 |
| B | LYS118 |
| B | TYR119 |
| site_id | AD2 |
| Number of Residues | 10 |
| Details | binding site for residue 9EP B 505 |
| Chain | Residue |
| B | SER91 |
| B | GLN147 |
| B | ASN179 |
| B | TYR248 |
| B | ASN316 |
| B | GLY344 |
| B | ALA345 |
| B | GLY347 |
| B | ASN370 |
| B | HOH730 |
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 | Active site: {"description":"Acyl-ester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU10102","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11478888","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12005439","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16506777","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35486701","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6795623","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9819201","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2000","firstPage":"10504","lastPage":"10512","volume":"122","journal":"J. Am. Chem. Soc.","title":"Crystal Structures of Substrate and Inhibitor Complexes with AmpC Beta-Lactamase: Possible Implications for Substrate-Assisted Catalysis.","authors":["Patera A.","Blaszczak L.C.","Shoichet B.K."],"citationCrossReferences":[{"database":"DOI","id":"10.1021/ja001676x"}]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16506777","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2000","firstPage":"10504","lastPage":"10512","volume":"122","journal":"J. Am. Chem. Soc.","title":"Crystal Structures of Substrate and Inhibitor Complexes with AmpC Beta-Lactamase: Possible Implications for Substrate-Assisted Catalysis.","authors":["Patera A.","Blaszczak L.C.","Shoichet B.K."],"citationCrossReferences":[{"database":"DOI","id":"10.1021/ja001676x"}]}},{"source":"PDB","id":"1FCN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FFY","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12005439","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12323371","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KVM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1LL9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16506777","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2FFY","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12005439","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12323371","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16506777","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2000","firstPage":"10504","lastPage":"10512","volume":"122","journal":"J. Am. Chem. Soc.","title":"Crystal Structures of Substrate and Inhibitor Complexes with AmpC Beta-Lactamase: Possible Implications for Substrate-Assisted Catalysis.","authors":["Patera A.","Blaszczak L.C.","Shoichet B.K."],"citationCrossReferences":[{"database":"DOI","id":"10.1021/ja001676x"}]}},{"source":"PDB","id":"1FCN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KVM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1LL9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FFY","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12005439","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KVM","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |






