6X9Y
The crystal structure of a Beta-lactamase from Escherichia coli CFT073
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 | 7 |
| Details | binding site for residue GOL A 401 |
| Chain | Residue |
| A | VAL236 |
| A | HIS237 |
| A | VAL238 |
| A | SER239 |
| A | GLY347 |
| A | GOL404 |
| A | HOH588 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 402 |
| Chain | Residue |
| A | TYR371 |
| A | PRO372 |
| A | ASN373 |
| A | HOH516 |
| A | ASP315 |
| A | ASN316 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 403 |
| Chain | Residue |
| A | LEU176 |
| A | GLU232 |
| A | GLY233 |
| A | LEU320 |
| A | ALA322 |
| A | HOH597 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 404 |
| Chain | Residue |
| A | GLN147 |
| A | ASN179 |
| A | ALA345 |
| A | THR346 |
| A | GLY347 |
| A | GOL401 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 405 |
| Chain | Residue |
| A | TRP120 |
| A | LEU188 |
| A | LYS191 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 A 406 |
| Chain | Residue |
| A | SER91 |
| A | TYR177 |
| A | LYS342 |
| A | THR343 |
| A | GLY344 |
| A | ALA345 |
| A | HOH504 |
| A | HOH605 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 401 |
| Chain | Residue |
| B | ASN316 |
| B | PRO372 |
| B | ASN373 |
| B | HOH502 |
| B | HOH511 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | binding site for residue GOL B 402 |
| Chain | Residue |
| B | SER91 |
| B | TYR177 |
| B | LYS342 |
| B | THR343 |
| B | GLY344 |
| B | ALA345 |
| B | HOH525 |
| B | HOH597 |
| B | HOH604 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 403 |
| Chain | Residue |
| B | GLN147 |
| B | ASN179 |
| B | ALA345 |
| B | SO4407 |
| B | HOH597 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue SRT B 404 |
| Chain | Residue |
| A | HIS135 |
| A | GLY172 |
| A | TRP287 |
| A | HOH530 |
| B | PRO327 |
| B | THR329 |
| B | HOH580 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 405 |
| Chain | Residue |
| B | TRP120 |
| B | ALA187 |
| B | LYS191 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 406 |
| Chain | Residue |
| B | GLU232 |
| B | GLY233 |
| B | LEU320 |
| B | ALA321 |
| B | ALA322 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 407 |
| Chain | Residue |
| B | VAL238 |
| B | SER239 |
| B | GLY347 |
| B | GOL403 |
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_FI2 |
| 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_FI3 |
| 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_FI4 |
| 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_FI5 |
| 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_FI6 |
| 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_FI7 |
| 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 |
