Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003914 | molecular_function | DNA (6-4) photolyase activity |
| A | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| A | 0006281 | biological_process | DNA repair |
| A | 0006290 | biological_process | pyrimidine dimer repair |
| A | 0009411 | biological_process | response to UV |
| A | 0016829 | molecular_function | lyase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003914 | molecular_function | DNA (6-4) photolyase activity |
| B | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| B | 0006281 | biological_process | DNA repair |
| B | 0006290 | biological_process | pyrimidine dimer repair |
| B | 0009411 | biological_process | response to UV |
| B | 0016829 | molecular_function | lyase activity |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003677 | molecular_function | DNA binding |
| C | 0003914 | molecular_function | DNA (6-4) photolyase activity |
| C | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| C | 0006281 | biological_process | DNA repair |
| C | 0006290 | biological_process | pyrimidine dimer repair |
| C | 0009411 | biological_process | response to UV |
| C | 0016829 | molecular_function | lyase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE IMD A 901 |
| Chain | Residue |
| A | TRP408 |
| A | PHE415 |
| A | TYR422 |
| B | LYS208 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE IMD A 902 |
| Chain | Residue |
| A | ASN330 |
| A | ASP378 |
| A | LEU379 |
| A | LYS492 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE IMD A 905 |
| Chain | Residue |
| A | PRO255 |
| A | TRP359 |
| A | PHE252 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MES A 920 |
| Chain | Residue |
| A | LYS244 |
| A | PRO245 |
| A | PRO292 |
| A | VAL293 |
| A | GLN298 |
| A | TRP301 |
| A | HIS364 |
| A | HIS368 |
| A | ASN405 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PO4 A 930 |
| Chain | Residue |
| A | PHE242 |
| A | GLU243 |
| site_id | AC6 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE FAD A 900 |
| Chain | Residue |
| A | LYS244 |
| A | THR257 |
| A | THR258 |
| A | VAL259 |
| A | MET260 |
| A | SER261 |
| A | LEU264 |
| A | GLN298 |
| A | TRP301 |
| A | ARG302 |
| A | PHE305 |
| A | TRP361 |
| A | HIS364 |
| A | ARG367 |
| A | HIS368 |
| A | PHE390 |
| A | LEU394 |
| A | ASP396 |
| A | SER397 |
| A | ASP398 |
| A | ILE401 |
| A | ASN402 |
| A | ASN405 |
| A | TRP406 |
| A | LEU409 |
| A | HOH3199 |
| A | HOH3354 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE IMD C 901 |
| Chain | Residue |
| C | TRP408 |
| C | PHE415 |
| C | ARG420 |
| C | TYR422 |
| C | HOH3357 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE IMD C 902 |
| Chain | Residue |
| C | ASN330 |
| C | ASP378 |
| C | ALA485 |
| C | LYS492 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE MES C 920 |
| Chain | Residue |
| C | LYS244 |
| C | PRO245 |
| C | PRO292 |
| C | TRP301 |
| C | HIS364 |
| C | HIS368 |
| C | ASN405 |
| C | TRP408 |
| C | FAD900 |
| C | HOH3135 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 C 930 |
| Chain | Residue |
| C | TRP238 |
| C | PHE242 |
| C | GLU243 |
| C | LYS246 |
| C | HOH3286 |
| site_id | BC2 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE FAD C 900 |
| Chain | Residue |
| C | HOH3013 |
| C | HOH3047 |
| C | HOH3136 |
| C | LYS244 |
| C | THR257 |
| C | THR258 |
| C | VAL259 |
| C | MET260 |
| C | SER261 |
| C | LEU264 |
| C | GLN298 |
| C | TRP301 |
| C | ARG302 |
| C | PHE305 |
| C | TRP361 |
| C | HIS364 |
| C | ARG367 |
| C | HIS368 |
| C | PHE390 |
| C | LEU394 |
| C | ASP396 |
| C | SER397 |
| C | ASP398 |
| C | ILE401 |
| C | ASN402 |
| C | ASN405 |
| C | TRP406 |
| C | LEU409 |
| C | MES920 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE IMD B 901 |
| Chain | Residue |
| B | TRP408 |
| B | PHE415 |
| B | ARG420 |
| B | TYR422 |
| C | LYS208 |
| site_id | BC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE IMD B 904 |
| Chain | Residue |
| B | LYS325 |
| B | TYR416 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE IMD B 905 |
| Chain | Residue |
| B | PHE252 |
| B | PRO255 |
| B | TRP359 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE IMD B 906 |
| Chain | Residue |
| B | LEU229 |
| B | THR230 |
| B | ILE233 |
| B | TYR273 |
| B | CYS277 |
| site_id | BC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MES B 920 |
| Chain | Residue |
| B | LYS244 |
| B | PRO245 |
| B | PRO292 |
| B | GLN298 |
| B | TRP301 |
| B | HIS364 |
| B | HIS368 |
| B | ASN405 |
| site_id | BC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PO4 B 930 |
| Chain | Residue |
| B | TRP238 |
| B | GLU243 |
| site_id | BC9 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE FAD B 900 |
| Chain | Residue |
| B | LYS244 |
| B | THR257 |
| B | THR258 |
| B | VAL259 |
| B | MET260 |
| B | SER261 |
| B | LEU264 |
| B | GLN298 |
| B | TRP301 |
| B | ARG302 |
| B | PHE305 |
| B | TRP361 |
| B | MET362 |
| B | HIS364 |
| B | ARG367 |
| B | HIS368 |
| B | PHE390 |
| B | LEU394 |
| B | ASP396 |
| B | SER397 |
| B | ASP398 |
| B | ILE401 |
| B | ASN402 |
| B | ASN405 |
| B | TRP406 |
| B | LEU409 |
| B | HOH3138 |
| B | HOH3153 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | PRO262 | |
| B | PRO262 | |
| C | PRO262 | |
| Chain | Residue | Details |
| A | TYR263 | |
| B | LYS317 | |
| B | PHE380 | |
| B | GLY386 | |
| B | PHE415 | |
| B | ILE421 | |
| C | TYR263 | |
| C | GLN276 | |
| C | LYS317 | |
| C | PHE380 | |
| C | GLY386 | |
| A | GLN276 | |
| C | PHE415 | |
| C | ILE421 | |
| A | LYS317 | |
| A | PHE380 | |
| A | GLY386 | |
| A | PHE415 | |
| A | ILE421 | |
| B | TYR263 | |
| B | GLN276 | |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | GLY320 | |
| A | PHE427 | |
| B | GLY320 | |
| B | PHE427 | |
| C | GLY320 | |
| C | PHE427 | |
| site_id | SWS_FT_FI4 |
| Number of Residues | 9 |
| Details | SITE: Electron transfer via tryptophanyl radical => ECO:0000250 |
| Chain | Residue | Details |
| A | TRP348 | |
| A | ASN402 | |
| A | ILE425 | |
| B | TRP348 | |
| B | ASN402 | |
| B | ILE425 | |
| C | TRP348 | |
| C | ASN402 | |
| C | ILE425 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1dnp |
| Chain | Residue | Details |
| A | TRP383 | |
| A | TRP406 | |
| A | TRP329 | |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1dnp |
| Chain | Residue | Details |
| B | TRP383 | |
| B | TRP406 | |
| B | TRP329 | |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1dnp |
| Chain | Residue | Details |
| C | TRP383 | |
| C | TRP406 | |
| C | TRP329 | |
