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 | 0006139 | biological_process | nucleobase-containing compound metabolic process |
A | 0006281 | biological_process | DNA repair |
A | 0006950 | biological_process | response to stress |
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 | 0006139 | biological_process | nucleobase-containing compound metabolic process |
B | 0006281 | biological_process | DNA repair |
B | 0006950 | biological_process | response to stress |
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
Chain | Residue | Details |
A | TYR268 | |
B | ASP427 | |
A | SER282 | |
A | LYS390 | |
A | ASN421 | |
A | ASP427 | |
B | TYR268 | |
B | SER282 | |
B | LYS390 | |
B | ASN421 | |
Chain | Residue | Details |
A | GLU319 | |
B | GLU319 | |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | SITE: Electron transfer via tryptophanyl radical => ECO:0000255 |
Chain | Residue | Details |
A | TRP378 | |
A | TRP399 | |
A | TRP406 | |
B | TRP378 | |
B | TRP399 | |
B | TRP406 | |
Chain | Residue | Details |
A | SER312 | |
B | SER312 | |