Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000719 | biological_process | photoreactive repair |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003904 | molecular_function | deoxyribodipyrimidine photo-lyase activity |
| A | 0003913 | molecular_function | DNA photolyase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0006281 | biological_process | DNA repair |
| A | 0006974 | biological_process | DNA damage response |
| A | 0009650 | biological_process | UV protection |
| A | 0016829 | molecular_function | lyase activity |
| A | 0071949 | molecular_function | FAD binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000719 | biological_process | photoreactive repair |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003904 | molecular_function | deoxyribodipyrimidine photo-lyase activity |
| B | 0003913 | molecular_function | DNA photolyase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0006281 | biological_process | DNA repair |
| B | 0006974 | biological_process | DNA damage response |
| B | 0009650 | biological_process | UV protection |
| B | 0016829 | molecular_function | lyase activity |
| B | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 701 |
| Chain | Residue |
| A | TRP241 |
| A | GLY283 |
| A | HIS388 |
| A | LYS390 |
| A | HOH691 |
| A | URE901 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 703 |
| Chain | Residue |
| A | GLN447 |
| A | HOH871 |
| A | HOH918 |
| A | HOH952 |
| A | SER184 |
| A | ASP221 |
| A | HIS445 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 705 |
| Chain | Residue |
| A | ARG46 |
| A | SER138 |
| A | LEU140 |
| A | PRO431 |
| A | HOH702 |
| A | HOH779 |
| A | HOH935 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 706 |
| Chain | Residue |
| A | GLU405 |
| A | ARG452 |
| A | PRO453 |
| A | HOH1293 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 707 |
| Chain | Residue |
| A | ASP148 |
| A | HOH655 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 708 |
| Chain | Residue |
| A | PRO78 |
| A | ARG79 |
| A | HOH802 |
| site_id | AC7 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE FAD A 801 |
| Chain | Residue |
| A | TYR268 |
| A | LEU281 |
| A | SER282 |
| A | GLY283 |
| A | LEU284 |
| A | SER285 |
| A | LEU288 |
| A | GLU319 |
| A | LEU320 |
| A | ARG323 |
| A | ARG324 |
| A | LYS390 |
| A | GLY393 |
| A | ARG396 |
| A | ASN421 |
| A | ASP427 |
| A | GLY428 |
| A | SER432 |
| A | GLY433 |
| A | GLY436 |
| A | HOH633 |
| A | HOH696 |
| A | HOH697 |
| A | HOH698 |
| A | HOH704 |
| A | HOH710 |
| A | HOH720 |
| A | HOH817 |
| A | HOH822 |
| A | HOH1047 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE URE A 901 |
| Chain | Residue |
| A | PRO278 |
| A | GLU384 |
| A | LYS390 |
| A | HIS392 |
| A | EDO701 |
| A | HOH760 |
| A | HOH1103 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE URE A 902 |
| Chain | Residue |
| A | TRP449 |
| A | LYS450 |
| A | ARG452 |
| A | GLY456 |
| A | ILE458 |
| A | ARG459 |
| A | TYR460 |
| A | HOH626 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE URE A 903 |
| Chain | Residue |
| A | ASP221 |
| A | LEU225 |
| A | HOH920 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE URE A 904 |
| Chain | Residue |
| A | PHE74 |
| A | ALA75 |
| A | LEU76 |
| A | PHE77 |
| A | LEU82 |
| A | LEU93 |
| A | HOH769 |
| A | HOH894 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE URE A 905 |
| Chain | Residue |
| A | PHE112 |
| A | LEU113 |
| A | PHE114 |
| A | PRO217 |
| A | GLU218 |
| A | HOH578 |
| A | HOH825 |
| A | HOH1027 |
| site_id | BC4 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE FAD B 801 |
| Chain | Residue |
| B | LEU288 |
| B | GLU319 |
| B | LEU320 |
| B | ARG323 |
| B | ARG324 |
| B | LYS390 |
| B | GLY393 |
| B | ARG396 |
| B | MET397 |
| B | ASN421 |
| B | ASP427 |
| B | GLY428 |
| B | SER432 |
| B | GLY433 |
| B | GLY436 |
| B | SER440 |
| B | HOH707 |
| B | HOH720 |
| B | HOH722 |
| B | HOH726 |
| B | HOH728 |
| B | HOH736 |
| B | HOH813 |
| B | HOH822 |
| B | HOH828 |
| B | TYR268 |
| B | LEU281 |
| B | SER282 |
| B | GLY283 |
| B | LEU284 |
| B | SER285 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE URE B 901 |
| Chain | Residue |
| B | PRO278 |
| B | GLU384 |
| B | LYS390 |
| B | HIS392 |
| B | HOH737 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE URE B 902 |
| Chain | Residue |
| B | TRP449 |
| B | LYS450 |
| B | ARG452 |
| B | ILE458 |
| B | ARG459 |
| B | TYR460 |
| site_id | BC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE URE B 904 |
| Chain | Residue |
| B | PHE74 |
| B | ALA75 |
| B | LEU76 |
| B | PHE77 |
| B | LEU82 |
| B | LEU93 |
| B | HOH785 |
| B | HOH875 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE URE B 905 |
| Chain | Residue |
| B | PHE112 |
| B | LEU113 |
| B | PHE114 |
| B | GLU218 |
| B | HOH830 |
Functional Information from PROSITE/UniProt
| site_id | PS01083 |
| Number of Residues | 15 |
| Details | DNA_PHOTOLYASES_2_1 DNA photolyases class 2 signature 1. FlEElVVRRELadNF |
| Chain | Residue | Details |
| A | PHE316-PHE330 | |
| site_id | PS01084 |
| Number of Residues | 20 |
| Details | DNA_PHOTOLYASES_2_2 DNA photolyases class 2 signature 2. GlHDqgWkERpVFGKIRYMN |
| Chain | Residue | Details |
| A | GLY443-ASN462 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 266 |
| Details | Domain: {"description":"Photolyase/cryptochrome alpha/beta"} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22170053","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3UMV","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P00914","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Site: {"description":"Electron transfer via tryptophanyl radical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18235036","evidenceCode":"ECO:0000269"}]} |
