6XTM
Crystal structure reveals non-coordinative binding of O2 to the copper center of the formylglycine-generating enzyme - FGE:Ag:S:O2 complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0018158 | biological_process | protein oxidation |
| A | 0043687 | biological_process | post-translational protein modification |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0120147 | molecular_function | formylglycine-generating oxidase activity |
| A | 1903136 | molecular_function | cuprous ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue OXY A 401 |
| Chain | Residue |
| A | TRP228 |
| A | SER266 |
| A | CYS269 |
| A | HIS293 |
| A | AG407 |
| A | HOH505 |
| C | CYS7 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue CA A 402 |
| Chain | Residue |
| A | GLY225 |
| A | VAL227 |
| A | GLU229 |
| A | GLY264 |
| A | GLY265 |
| A | ASN222 |
| A | VAL223 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 403 |
| Chain | Residue |
| A | ASN188 |
| A | ILE189 |
| A | ASP202 |
| A | TYR204 |
| A | HOH555 |
| A | HOH579 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 404 |
| Chain | Residue |
| A | PRO131 |
| A | ASN132 |
| A | HIS133 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 405 |
| Chain | Residue |
| A | PHE38 |
| A | PRO39 |
| A | GLU40 |
| C | THR4 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 406 |
| Chain | Residue |
| A | ASN177 |
| A | GLU178 |
| A | PRO181 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue AG A 407 |
| Chain | Residue |
| A | CYS269 |
| A | CYS274 |
| A | ARG276 |
| A | OXY401 |
| C | CYS7 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue SOA C 101 |
| Chain | Residue |
| A | ARG248 |
| A | ILE249 |
| A | TYR273 |
| C | ALA2 |
| C | THR3 |
| C | PRO5 |
| C | HOH212 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"28544744","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5NXL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5NYY","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27862795","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28544744","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5NXL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5NYY","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
