4E3L
Crystal structure of AmpC beta-lactamase in complex with a 3-chloro-4-tetrazolyl benzene sulfonamide boronic acid inhibitor
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 | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| A | 0042597 | cellular_component | periplasmic space |
| 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 | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE 0NB A 401 |
| Chain | Residue |
| A | SER64 |
| A | HOH788 |
| A | TYR150 |
| A | ASN152 |
| A | VAL211 |
| A | SER212 |
| A | ALA318 |
| A | GLY320 |
| A | HOH785 |
| A | HOH787 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 A 402 |
| Chain | Residue |
| A | PHE41 |
| A | THR42 |
| A | HOH577 |
| A | HOH601 |
| A | HOH759 |
| A | HOH813 |
| B | GLY116 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 A 403 |
| Chain | Residue |
| A | THR262 |
| A | GLY263 |
| A | PRO297 |
| A | HOH606 |
| B | TYR45 |
| B | LYS51 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 A 404 |
| Chain | Residue |
| A | TRP93 |
| A | LEU157 |
| A | LYS164 |
| A | HOH616 |
| A | HOH682 |
| A | HOH768 |
| A | HOH797 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 405 |
| Chain | Residue |
| A | PRO140 |
| A | ALA141 |
| A | TRP142 |
| A | ALA143 |
| A | HOH771 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE 0NB B 401 |
| Chain | Residue |
| A | LEU85 |
| A | GLN250 |
| A | LEU254 |
| A | SER257 |
| A | TYR259 |
| A | PRO304 |
| A | HOH534 |
| B | GLN250 |
| B | GLN253 |
| B | LEU254 |
| B | SER257 |
| B | PRO303 |
| B | PRO304 |
| B | PRO306 |
| B | HOH628 |
| B | HOH641 |
| B | HOH758 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE 0NB B 402 |
| Chain | Residue |
| B | SER64 |
| B | GLN120 |
| B | TYR150 |
| B | ASN152 |
| B | VAL211 |
| B | SER212 |
| B | GLY317 |
| B | ALA318 |
| B | GLY320 |
| B | HOH739 |
| B | HOH741 |
| B | HOH747 |
| B | HOH755 |
| B | HOH774 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 B 403 |
| Chain | Residue |
| A | ARG133 |
| A | HIS186 |
| A | HOH711 |
| A | HOH743 |
| A | HOH748 |
| B | LYS290 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PO4 B 404 |
| Chain | Residue |
| B | ARG80 |
| B | HOH567 |
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 | PHE60-LYS67 |
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 |
