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 | |