2HDU
AmpC beta-lactamase in complex with 2-acetamidothiophene-3-carboxylic acid
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 | 3 |
| Details | BINDING SITE FOR RESIDUE K B 2001 |
| Chain | Residue |
| A | PRO303 |
| B | PRO303 |
| B | HOH2256 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 B 2002 |
| Chain | Residue |
| A | HOH1428 |
| A | HOH1441 |
| B | LYS290 |
| B | HOH2197 |
| A | ARG133 |
| A | HIS186 |
| A | HOH1213 |
| A | HOH1245 |
| A | HOH1378 |
| A | HOH1423 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE F12 B 1001 |
| Chain | Residue |
| B | SER64 |
| B | GLN120 |
| B | ASN152 |
| B | TYR221 |
| B | GLY317 |
| B | ALA318 |
| B | F121006 |
| B | HOH2028 |
| B | HOH2111 |
| B | HOH2117 |
| B | HOH2343 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE F12 B 1002 |
| Chain | Residue |
| A | GLN250 |
| A | GLN253 |
| A | LEU254 |
| A | SER257 |
| A | PRO304 |
| A | PRO306 |
| A | HOH1413 |
| A | HOH1473 |
| B | GLN250 |
| B | LEU254 |
| B | SER257 |
| B | PRO304 |
| B | PRO306 |
| B | HOH2101 |
| B | HOH2483 |
| B | HOH2484 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE F12 B 1003 |
| Chain | Residue |
| A | GLN56 |
| A | HOH1025 |
| B | LEU119 |
| B | LEU293 |
| B | F121006 |
| B | HOH2118 |
| B | HOH2128 |
| B | HOH2138 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE F12 A 1004 |
| Chain | Residue |
| A | THR262 |
| A | GLY263 |
| A | PRO297 |
| A | VAL298 |
| A | LYS299 |
| A | HOH1235 |
| A | HOH1255 |
| B | TYR45 |
| B | LYS51 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE F12 B 1005 |
| Chain | Residue |
| A | HOH1329 |
| B | SER282 |
| B | ASN285 |
| B | GLY286 |
| B | ILE291 |
| B | ARG296 |
| B | HOH2141 |
| B | HOH2265 |
| B | HOH2319 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE F12 B 1006 |
| Chain | Residue |
| B | GLN120 |
| B | ASN289 |
| B | LEU293 |
| B | THR319 |
| B | ASN343 |
| B | F121001 |
| B | F121003 |
| B | HOH2331 |
| site_id | AC9 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE F12 B 1008 |
| Chain | Residue |
| A | PRO118 |
| A | PHE134 |
| A | TRP138 |
| A | GLN139 |
| A | HOH1038 |
| A | HOH1174 |
| B | HIS13 |
| B | ARG14 |
| B | HOH2082 |
| B | HOH2166 |
| B | HOH2183 |
| B | HOH2263 |
| B | HOH2283 |
| B | HOH2418 |
| site_id | BC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE F12 A 1009 |
| Chain | Residue |
| A | TYR221 |
| A | ALA318 |
| A | GLY320 |
| A | ASN343 |
| A | HOH1359 |
| A | HOH1409 |
| A | HOH1420 |
| A | HOH1421 |
| A | HOH1457 |
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 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1xx2 |
| Chain | Residue | Details |
| A | GLU272 | |
| A | SER64 | |
| A | LYS315 | |
| A | TYR150 | |
| A | LYS67 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1xx2 |
| Chain | Residue | Details |
| B | GLU272 | |
| B | SER64 | |
| B | LYS315 | |
| B | TYR150 | |
| B | LYS67 |
