6R73
Structure of IMP-13 metallo-beta-lactamase complexed with hydrolysed meropenem
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0008800 | molecular_function | beta-lactamase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0017001 | biological_process | antibiotic catabolic process |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0046677 | biological_process | response to antibiotic |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0008800 | molecular_function | beta-lactamase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0017001 | biological_process | antibiotic catabolic process |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0046677 | biological_process | response to antibiotic |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | binding site for residue LMP A 301 |
| Chain | Residue |
| A | TRP28 |
| A | ASN167 |
| A | HIS197 |
| A | ZN302 |
| A | ZN303 |
| A | HOH440 |
| B | TRP28 |
| A | HIS77 |
| A | HIS79 |
| A | ASP81 |
| A | HIS139 |
| A | CYS158 |
| A | LYS161 |
| A | GLY164 |
| A | GLY166 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 302 |
| Chain | Residue |
| A | HIS77 |
| A | HIS79 |
| A | HIS139 |
| A | LMP301 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 303 |
| Chain | Residue |
| A | ASP81 |
| A | CYS158 |
| A | HIS197 |
| A | LMP301 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 302 |
| Chain | Residue |
| B | HIS77 |
| B | HIS79 |
| B | HIS139 |
| B | LMP301 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 303 |
| Chain | Residue |
| B | ASP81 |
| B | CYS158 |
| B | HIS197 |
| B | LMP301 |
| site_id | AC6 |
| Number of Residues | 20 |
| Details | binding site for Di-peptide LMP B 301 and LYS B 161 |
| Chain | Residue |
| A | TRP28 |
| B | TRP28 |
| B | HIS79 |
| B | SER80 |
| B | ASP81 |
| B | HIS139 |
| B | CYS158 |
| B | PHE159 |
| B | ILE160 |
| B | PRO162 |
| B | HIS163 |
| B | GLY164 |
| B | LEU165 |
| B | GLY166 |
| B | ASN167 |
| B | HIS197 |
| B | THR209 |
| B | GLN212 |
| B | ZN302 |
| B | ZN303 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"32205343","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2020","submissionDatabase":"PDB data bank","title":"Structure of IMP-13 metallo-beta-lactamase complexed with citrate anion.","authors":["Zak K.M.","Zhou R.X.","Softley C.A.","Bostock M.J.","Sattler M.","Popowicz G.M."]}},{"source":"PDB","id":"6R73","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6R79","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6RZR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6RZS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6S0H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6YI4","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P52699","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"32205343","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
