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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 514 |
| Chain | Residue |
| A | ASP359 |
| A | FAD510 |
| A | HEZ518 |
| A | HOH579 |
| A | HOH580 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 515 |
| Chain | Residue |
| A | ASN238 |
| A | THR246 |
| A | HIS358 |
| A | MG516 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 516 |
| Chain | Residue |
| A | LYS241 |
| A | SER244 |
| A | THR246 |
| A | MG515 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 517 |
| site_id | AC5 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE FAD A 510 |
| Chain | Residue |
| A | TYR235 |
| A | THR247 |
| A | SER248 |
| A | PHE249 |
| A | LEU250 |
| A | SER251 |
| A | LEU254 |
| A | PHE290 |
| A | SER293 |
| A | ARG297 |
| A | TRP356 |
| A | ASP359 |
| A | ARG362 |
| A | VAL363 |
| A | SER366 |
| A | LEU388 |
| A | ASP390 |
| A | ALA391 |
| A | ASP392 |
| A | SER395 |
| A | ASP396 |
| A | MG514 |
| A | HEZ518 |
| A | HOH520 |
| A | HOH521 |
| A | HOH539 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NDS A 512 |
| Chain | Residue |
| A | ALA212 |
| A | TRP213 |
| A | SER214 |
| A | ALA223 |
| A | PHE249 |
| A | HIS253 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE HEZ A 518 |
| Chain | Residue |
| A | SER395 |
| A | LEU398 |
| A | GLY399 |
| A | TYR402 |
| A | FAD510 |
| A | MG514 |
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 | THR339-LEU351 | |
| site_id | PS00691 |
| Number of Residues | 20 |
| Details | DNA_PHOTOLYASES_1_2 DNA photolyases class 1 signature 2. DRiRVVvSSFFvKvLqlpWR |
| Chain | Residue | Details |
| A | ASP359-ARG378 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15299148","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1U3C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1U3D","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15299148","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1U3C","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15299148","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1U3D","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Involved in electron transfer from the protein surface to the FAD cofactor","evidences":[{"source":"PubMed","id":"26313597","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22421133","evidenceCode":"ECO:0000303"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Site: {"description":"Involved in electron transfer from the protein surface to the FAD cofactor","evidences":[{"source":"PubMed","id":"22421133","evidenceCode":"ECO:0000303"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1dnp |
| Chain | Residue | Details |
| A | TRP400 | |
| A | TRP377 | |
| A | TRP324 | |
