Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0009785 | biological_process | blue light signaling pathway |
| A | 0009882 | molecular_function | blue light photoreceptor activity |
| B | 0009785 | biological_process | blue light signaling pathway |
| B | 0009882 | molecular_function | blue light photoreceptor activity |
| C | 0009785 | biological_process | blue light signaling pathway |
| C | 0009882 | molecular_function | blue light photoreceptor activity |
| D | 0009785 | biological_process | blue light signaling pathway |
| D | 0009882 | molecular_function | blue light photoreceptor activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | binding site for residue FAD A 501 |
| Chain | Residue |
| A | TYR232 |
| A | LEU293 |
| A | ARG294 |
| A | TRP353 |
| A | ASN356 |
| A | ARG359 |
| A | LEU385 |
| A | ASP387 |
| A | ALA388 |
| A | ASP389 |
| A | CYS392 |
| A | THR244 |
| A | ASP393 |
| A | GLY396 |
| A | SER245 |
| A | LEU246 |
| A | LEU247 |
| A | SER248 |
| A | LEU251 |
| A | GLY290 |
| A | ILE291 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 502 |
| Chain | Residue |
| A | GLY464 |
| A | THR465 |
| A | ASN466 |
| A | TYR467 |
| A | ALA468 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | ARG13 |
| A | ILE37 |
| A | GLU43 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 504 |
| Chain | Residue |
| A | ARG332 |
| A | GLN333 |
| A | TRP349 |
| A | TYR380 |
| B | GLY460 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue GOL A 505 |
| Chain | Residue |
| A | ARG266 |
| D | PRO171 |
| site_id | AC6 |
| Number of Residues | 21 |
| Details | binding site for residue FAD B 501 |
| Chain | Residue |
| B | TYR232 |
| B | THR244 |
| B | SER245 |
| B | LEU246 |
| B | LEU247 |
| B | SER248 |
| B | LEU251 |
| B | PHE287 |
| B | GLY290 |
| B | ILE291 |
| B | LEU293 |
| B | ARG294 |
| B | TRP353 |
| B | ASN356 |
| B | ARG359 |
| B | ASP387 |
| B | ASP389 |
| B | CYS392 |
| B | ASP393 |
| B | GLY396 |
| B | GOL503 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 502 |
| Chain | Residue |
| B | ARG12 |
| B | ARG13 |
| B | PHE36 |
| B | ILE37 |
| B | GLU43 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 503 |
| Chain | Residue |
| B | TYR232 |
| B | LEU286 |
| B | ARG357 |
| B | FAD501 |
| site_id | AC9 |
| Number of Residues | 23 |
| Details | binding site for residue FAD C 501 |
| Chain | Residue |
| C | TYR232 |
| C | THR244 |
| C | SER245 |
| C | LEU246 |
| C | LEU247 |
| C | SER248 |
| C | LEU251 |
| C | PHE287 |
| C | GLY290 |
| C | ILE291 |
| C | LEU293 |
| C | ARG294 |
| C | TRP353 |
| C | MET354 |
| C | HIS355 |
| C | ASN356 |
| C | ARG359 |
| C | VAL360 |
| C | ASP387 |
| C | ASP389 |
| C | CYS392 |
| C | GLY396 |
| C | GOL505 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue GOL C 502 |
| Chain | Residue |
| C | THR465 |
| C | ASN466 |
| D | THR465 |
| D | ASN466 |
| site_id | AD2 |
| Number of Residues | 2 |
| Details | binding site for residue GOL C 503 |
| Chain | Residue |
| B | CYS264 |
| C | HIS260 |
| site_id | AD3 |
| Number of Residues | 1 |
| Details | binding site for residue GOL C 505 |
| site_id | AD4 |
| Number of Residues | 1 |
| Details | binding site for residue GOL C 506 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue GOL C 507 |
| Chain | Residue |
| C | SER108 |
| C | ARG111 |
| C | ARG12 |
| C | ILE37 |
| site_id | AD6 |
| Number of Residues | 20 |
| Details | binding site for residue FAD D 501 |
| Chain | Residue |
| D | TYR232 |
| D | THR244 |
| D | SER245 |
| D | LEU246 |
| D | LEU247 |
| D | SER248 |
| D | GLY290 |
| D | ILE291 |
| D | LEU293 |
| D | ARG294 |
| D | TRP353 |
| D | ASN356 |
| D | ARG359 |
| D | VAL360 |
| D | SER363 |
| D | ASP387 |
| D | ASP389 |
| D | CYS392 |
| D | ASP393 |
| D | GLY396 |
| site_id | AD7 |
| Number of Residues | 2 |
| Details | binding site for residue GOL D 502 |
| Chain | Residue |
| C | LYS457 |
| D | GLU199 |
| site_id | AD8 |
| Number of Residues | 1 |
| Details | binding site for residue GOL D 503 |
| site_id | AD9 |
| Number of Residues | 7 |
| Details | binding site for residue GOL D 504 |
| Chain | Residue |
| D | ARG12 |
| D | ILE37 |
| D | TRP38 |
| D | GLU43 |
| D | LEU103 |
| D | SER108 |
| D | ARG111 |
Functional Information from PROSITE/UniProt
| site_id | PS00394 |
| Number of Residues | 13 |
| Details | DNA_PHOTOLYASES_1_1 DNA photolyases class 1 signature 1. TGyPLVDAgMReL |
| Chain | Residue | Details |
| A | THR336-LEU348 | |
| site_id | PS00691 |
| Number of Residues | 20 |
| Details | DNA_PHOTOLYASES_1_2 DNA photolyases class 1 signature 2. NRiRVIvSSFAvKfLllpWK |
| Chain | Residue | Details |
| A | ASN356-LYS375 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | TYR232 | |
| C | THR244 | |
| C | ASN356 | |
| C | ASP387 | |
| D | TYR232 | |
| D | THR244 | |
| D | ASN356 | |
| D | ASP387 | |
| A | THR244 | |
| A | ASN356 | |
| A | ASP387 | |
| B | TYR232 | |
| B | THR244 | |
| B | ASN356 | |
| B | ASP387 | |
| C | TYR232 | |
| Chain | Residue | Details |
| A | ASN235 | |
| C | SER243 | |
| C | HIS355 | |
| C | ASP406 | |
| D | ASN235 | |
| D | SER243 | |
| D | HIS355 | |
| D | ASP406 | |
| A | SER243 | |
| A | HIS355 | |
| A | ASP406 | |
| B | ASN235 | |
| B | SER243 | |
| B | HIS355 | |
| B | ASP406 | |
| C | ASN235 | |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | SITE: Involved in electron transfer from the protein surface to the FAD cofactor => ECO:0000269|PubMed:25428980 |
| Chain | Residue | Details |
| A | TRP321 | |
| D | TRP321 | |
| D | TRP374 | |
| D | TRP397 | |
| A | TRP374 | |
| A | TRP397 | |
| B | TRP321 | |
| B | TRP374 | |
| B | TRP397 | |
| C | TRP321 | |
| C | TRP374 | |
| C | TRP397 | |
