6RZR
Structure of IMP-13 metallo-beta-lactamase complexed with hydrolysed imipenem
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 | 4 |
| Details | binding site for residue ZN A 301 |
| Chain | Residue |
| A | HIS77 |
| A | HIS79 |
| A | HIS139 |
| A | 8YF311 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 302 |
| Chain | Residue |
| A | ASP81 |
| A | CYS158 |
| A | HIS197 |
| A | 8YF311 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 303 |
| Chain | Residue |
| A | PRO135 |
| A | GLY136 |
| A | ILE182 |
| A | HOH439 |
| B | TRP28 |
| B | 8YF307 |
| A | TYR134 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 304 |
| Chain | Residue |
| A | VAL64 |
| A | GLU69 |
| A | ILE70 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 305 |
| Chain | Residue |
| A | TRP147 |
| A | PRO149 |
| A | LYS152 |
| A | EDO306 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 306 |
| Chain | Residue |
| A | EDO305 |
| A | HOH409 |
| A | HOH443 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 307 |
| Chain | Residue |
| A | GLY15 |
| A | LEU39 |
| A | LEU148 |
| A | GLU150 |
| A | SER151 |
| A | HOH436 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 308 |
| Chain | Residue |
| A | ASN103 |
| A | GLN113 |
| A | ALA114 |
| A | LYS115 |
| A | SER117 |
| A | HOH403 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 309 |
| Chain | Residue |
| A | GLN141 |
| A | ASP170 |
| A | ALA171 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 310 |
| Chain | Residue |
| A | LEU7 |
| A | LYS58 |
| A | TRP62 |
| A | HOH421 |
| site_id | AD2 |
| Number of Residues | 14 |
| Details | binding site for residue 8YF A 311 |
| Chain | Residue |
| A | HIS77 |
| A | HIS79 |
| A | SER80 |
| A | ASP81 |
| A | HIS139 |
| A | CYS158 |
| A | LYS161 |
| A | LEU165 |
| A | GLY166 |
| A | ASN167 |
| A | HIS197 |
| A | ZN301 |
| A | ZN302 |
| A | HOH497 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 301 |
| Chain | Residue |
| B | HIS77 |
| B | HIS79 |
| B | HIS139 |
| B | 8YF307 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 302 |
| Chain | Residue |
| B | ASP81 |
| B | CYS158 |
| B | HIS197 |
| B | 8YF307 |
| site_id | AD5 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 303 |
| Chain | Residue |
| A | TRP28 |
| B | VAL121 |
| B | PHE133 |
| B | TYR134 |
| B | PRO135 |
| B | GLY136 |
| B | HOH414 |
| site_id | AD6 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 304 |
| Chain | Residue |
| A | SER99 |
| A | HOH418 |
| B | VAL30 |
| B | THR32 |
| B | HOH443 |
| site_id | AD7 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 305 |
| Chain | Residue |
| B | TYR116 |
| B | SER117 |
| site_id | AD8 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 306 |
| Chain | Residue |
| B | HIS34 |
| B | GLU199 |
| B | LYS200 |
| site_id | AD9 |
| Number of Residues | 23 |
| Details | binding site for residue 8YF B 307 |
| Chain | Residue |
| B | GLY166 |
| B | ASN167 |
| B | HIS197 |
| B | ZN301 |
| B | ZN302 |
| B | HOH407 |
| B | HOH423 |
| A | VAL121 |
| A | EDO303 |
| A | HOH402 |
| B | VAL25 |
| B | TRP28 |
| B | VAL30 |
| B | VAL31 |
| B | THR32 |
| B | HIS77 |
| B | HIS79 |
| B | SER80 |
| B | ASP81 |
| B | HIS139 |
| B | CYS158 |
| B | LYS161 |
| B | LEU165 |
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 |
