6PZ0
Crystal structure of oxidized iodotyrosine deiodinase (IYD) bound to FMN and L-Tyrosine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006570 | biological_process | tyrosine metabolic process |
| A | 0010181 | molecular_function | FMN binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0072545 | molecular_function | L-tyrosine binding |
| A | 0140616 | molecular_function | iodotyrosine deiodinase activity |
| B | 0006570 | biological_process | tyrosine metabolic process |
| B | 0010181 | molecular_function | FMN binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0072545 | molecular_function | L-tyrosine binding |
| B | 0140616 | molecular_function | iodotyrosine deiodinase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | binding site for residue FMN A 301 |
| Chain | Residue |
| A | LYS12 |
| A | LYS173 |
| A | TYR174 |
| A | ARG176 |
| A | TYR302 |
| A | CL303 |
| A | HOH436 |
| A | HOH443 |
| A | HOH455 |
| A | HOH470 |
| B | PRO38 |
| A | THR13 |
| B | SER39 |
| B | GLY40 |
| B | ASN42 |
| B | GLU115 |
| B | SER116 |
| A | ARG15 |
| A | TRP82 |
| A | PHE88 |
| A | VAL136 |
| A | PRO137 |
| A | TYR138 |
| A | THR139 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue TYR A 302 |
| Chain | Residue |
| A | GLU68 |
| A | TYR72 |
| A | TRP82 |
| A | LEU83 |
| A | LYS92 |
| A | TYR138 |
| A | THR139 |
| A | FMN301 |
| A | HOH463 |
| B | GLY40 |
| B | MET41 |
| B | TYR112 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 303 |
| Chain | Residue |
| A | ARG11 |
| A | THR13 |
| A | PRO137 |
| A | FMN301 |
| B | PRO38 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | binding site for residue CL A 304 |
| Chain | Residue |
| A | ARG157 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 305 |
| Chain | Residue |
| A | ARG15 |
| A | ARG16 |
| A | PRO170 |
| A | LYS171 |
| A | HOH454 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 306 |
| Chain | Residue |
| A | TRP82 |
| A | LYS86 |
| B | ASN42 |
| B | ASN177 |
| site_id | AC7 |
| Number of Residues | 23 |
| Details | binding site for residue FMN B 301 |
| Chain | Residue |
| A | PRO38 |
| A | SER39 |
| A | GLY40 |
| A | ASN42 |
| A | TYR112 |
| A | SER116 |
| B | LYS12 |
| B | THR13 |
| B | ARG15 |
| B | PHE88 |
| B | VAL136 |
| B | PRO137 |
| B | TYR138 |
| B | THR139 |
| B | LYS173 |
| B | TYR174 |
| B | ARG176 |
| B | TYR302 |
| B | CL303 |
| B | HOH447 |
| B | HOH457 |
| B | HOH461 |
| B | HOH473 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue TYR B 302 |
| Chain | Residue |
| A | MET41 |
| B | GLU68 |
| B | TYR72 |
| B | LEU83 |
| B | LYS92 |
| B | TYR138 |
| B | THR139 |
| B | FMN301 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue CL B 303 |
| Chain | Residue |
| A | PRO38 |
| B | ARG11 |
| B | THR13 |
| B | PRO137 |
| B | FMN301 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 304 |
| Chain | Residue |
| A | ASN42 |
| A | ASN177 |
| B | TRP82 |
| B | LYS86 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"6PZ0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6Q1B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6Q1L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6TYK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"34748729","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6PZ0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6TYK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
