Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016491 | molecular_function | oxidoreductase activity |
B | 0016491 | molecular_function | oxidoreductase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE FAD A 301 |
Chain | Residue |
A | TYR40 |
A | ASN82 |
A | GLY84 |
A | LEU85 |
A | VAL86 |
A | SER87 |
A | THR128 |
A | GLU234 |
A | PHE236 |
A | HOH422 |
A | HOH436 |
A | ARG56 |
A | HOH457 |
A | HOH467 |
B | ASP3 |
B | ARG5 |
B | ARG53 |
B | TYR103 |
B | HOH538 |
A | GLN57 |
A | TYR58 |
A | SER59 |
A | SER72 |
A | VAL73 |
A | LYS74 |
A | GLU76 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL A 302 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 303 |
Chain | Residue |
A | ARG2 |
A | ARG2 |
A | GLY4 |
A | LEU102 |
A | TYR103 |
A | ALA104 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 304 |
Chain | Residue |
A | ASP108 |
A | PHE109 |
A | TYR233 |
site_id | AC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL A 305 |
Chain | Residue |
A | ARG114 |
A | HOH491 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL A 306 |
Chain | Residue |
A | LYS142 |
A | SER143 |
site_id | AC7 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL A 307 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 308 |
Chain | Residue |
A | TYR89 |
A | ASN93 |
A | HOH462 |
A | HOH504 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 401 |
Chain | Residue |
B | GLU48 |
B | TYR89 |
B | ASN93 |
B | HOH516 |
B | HOH535 |
B | HOH596 |
site_id | BC1 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE FAD B 402 |
Chain | Residue |
B | TYR40 |
B | ARG56 |
B | GLN57 |
B | TYR58 |
B | SER59 |
B | SER72 |
B | VAL73 |
B | LYS74 |
B | GLU76 |
B | GLY84 |
B | LEU85 |
B | VAL86 |
B | SER87 |
B | VAL125 |
B | THR128 |
B | PHE236 |
B | HIS239 |
B | HOH511 |
B | HOH523 |
B | HOH564 |
B | HOH565 |
B | HOH572 |
site_id | BC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 403 |
Chain | Residue |
A | ALA168 |
B | ASP108 |
B | PHE109 |
B | PHE110 |
B | VAL112 |
B | ARG114 |
B | TYR206 |
B | HIS232 |
site_id | BC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 404 |
Chain | Residue |
A | PRO238 |
B | TYR40 |
B | ILE41 |
B | GLY42 |
B | GLN57 |
B | ALA104 |
B | ALA106 |
site_id | BC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL B 406 |
Chain | Residue |
B | LYS74 |
B | VAL125 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | TYR40 | |
A | ARG56 | |
A | GLY124 | |
A | VAL235 | |
B | TYR40 | |
B | ARG56 | |
B | GLY124 | |
B | VAL235 | |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | SITE: Influences the redox potential of the prosthetic heme and FAD groups => ECO:0000250 |
Chain | Residue | Details |
A | GLU234 | |
B | GLU234 | |