2VTB
Structure of cryptochrome 3 - DNA complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 0005524 | molecular_function | ATP binding |
A | 0005739 | cellular_component | mitochondrion |
A | 0006139 | biological_process | nucleobase-containing compound metabolic process |
A | 0006281 | biological_process | DNA repair |
A | 0006950 | biological_process | response to stress |
A | 0009507 | cellular_component | chloroplast |
A | 0009881 | molecular_function | photoreceptor activity |
A | 0071949 | molecular_function | FAD 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 | 0005524 | molecular_function | ATP binding |
B | 0005739 | cellular_component | mitochondrion |
B | 0006139 | biological_process | nucleobase-containing compound metabolic process |
B | 0006281 | biological_process | DNA repair |
B | 0006950 | biological_process | response to stress |
B | 0009507 | cellular_component | chloroplast |
B | 0009881 | molecular_function | photoreceptor activity |
B | 0071949 | molecular_function | FAD binding |
C | 0000719 | biological_process | photoreactive repair |
C | 0003677 | molecular_function | DNA binding |
C | 0003904 | molecular_function | deoxyribodipyrimidine photo-lyase activity |
C | 0003913 | molecular_function | DNA photolyase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0005739 | cellular_component | mitochondrion |
C | 0006139 | biological_process | nucleobase-containing compound metabolic process |
C | 0006281 | biological_process | DNA repair |
C | 0006950 | biological_process | response to stress |
C | 0009507 | cellular_component | chloroplast |
C | 0009881 | molecular_function | photoreceptor activity |
C | 0071949 | molecular_function | FAD binding |
D | 0000719 | biological_process | photoreactive repair |
D | 0003677 | molecular_function | DNA binding |
D | 0003904 | molecular_function | deoxyribodipyrimidine photo-lyase activity |
D | 0003913 | molecular_function | DNA photolyase activity |
D | 0005524 | molecular_function | ATP binding |
D | 0005739 | cellular_component | mitochondrion |
D | 0006139 | biological_process | nucleobase-containing compound metabolic process |
D | 0006281 | biological_process | DNA repair |
D | 0006950 | biological_process | response to stress |
D | 0009507 | cellular_component | chloroplast |
D | 0009881 | molecular_function | photoreceptor activity |
D | 0071949 | molecular_function | FAD binding |
E | 0000719 | biological_process | photoreactive repair |
E | 0003677 | molecular_function | DNA binding |
E | 0003904 | molecular_function | deoxyribodipyrimidine photo-lyase activity |
E | 0003913 | molecular_function | DNA photolyase activity |
E | 0005524 | molecular_function | ATP binding |
E | 0005739 | cellular_component | mitochondrion |
E | 0006139 | biological_process | nucleobase-containing compound metabolic process |
E | 0006281 | biological_process | DNA repair |
E | 0006950 | biological_process | response to stress |
E | 0009507 | cellular_component | chloroplast |
E | 0009881 | molecular_function | photoreceptor activity |
E | 0071949 | molecular_function | FAD binding |
F | 0000719 | biological_process | photoreactive repair |
F | 0003677 | molecular_function | DNA binding |
F | 0003904 | molecular_function | deoxyribodipyrimidine photo-lyase activity |
F | 0003913 | molecular_function | DNA photolyase activity |
F | 0005524 | molecular_function | ATP binding |
F | 0005739 | cellular_component | mitochondrion |
F | 0006139 | biological_process | nucleobase-containing compound metabolic process |
F | 0006281 | biological_process | DNA repair |
F | 0006950 | biological_process | response to stress |
F | 0009507 | cellular_component | chloroplast |
F | 0009881 | molecular_function | photoreceptor activity |
F | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE FAD A 998 |
Chain | Residue |
A | TYR272 |
A | PHE388 |
A | ASN391 |
A | ARG394 |
A | GLN395 |
A | LEU420 |
A | ASP422 |
A | TYR423 |
A | ASP424 |
A | SER427 |
A | ASN428 |
A | SER285 |
A | ASN431 |
A | TRP432 |
A | HOH2173 |
A | HOH2174 |
A | HOH2240 |
A | HOH2269 |
A | HOH2270 |
G | DT2 |
G | TCP3 |
A | THR286 |
A | LYS287 |
A | PHE288 |
A | SER289 |
A | LEU292 |
A | GLU325 |
A | ARG329 |
site_id | AC2 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE MHF A 999 |
Chain | Residue |
A | HIS83 |
A | LYS89 |
A | CYS146 |
A | SER147 |
A | GLU148 |
A | GLU149 |
A | ASN341 |
A | PHE344 |
A | HIS345 |
A | GLU417 |
A | TYR423 |
A | PRO425 |
A | TYR429 |
A | HOH2271 |
A | HOH2272 |
B | PHE188 |
B | ASP189 |
B | ASP192 |
B | LYS338 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CL A 1501 |
Chain | Residue |
A | ARG51 |
A | ASP54 |
A | ASP56 |
A | HIS142 |
A | ARG300 |
A | HOH2190 |
site_id | AC4 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE FAD B 998 |
Chain | Residue |
B | TYR272 |
B | SER285 |
B | THR286 |
B | LYS287 |
B | PHE288 |
B | SER289 |
B | LEU292 |
B | GLU325 |
B | ARG329 |
B | PHE332 |
B | PHE388 |
B | ASN391 |
B | ARG394 |
B | LEU420 |
B | ASP422 |
B | TYR423 |
B | ASP424 |
B | ASN428 |
B | ASN431 |
B | TRP432 |
B | HOH2123 |
B | HOH2124 |
B | HOH2158 |
B | HOH2168 |
B | HOH2176 |
H | DT2 |
H | TCP3 |
site_id | AC5 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE MHF B 999 |
Chain | Residue |
A | PHE188 |
A | ASP189 |
A | LYS338 |
A | HOH2129 |
B | HIS83 |
B | LYS89 |
B | CYS146 |
B | SER147 |
B | GLU148 |
B | GLU149 |
B | ASN341 |
B | PHE344 |
B | HIS345 |
B | GLU417 |
B | TYR423 |
B | PRO425 |
B | TYR429 |
B | HOH2178 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL B 1498 |
Chain | Residue |
B | ASP54 |
B | ASP56 |
B | HIS142 |
B | ARG300 |
B | ARG51 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL B 1499 |
Chain | Residue |
B | GLY281 |
B | HOH2108 |
B | HOH2175 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACT B 1500 |
Chain | Residue |
B | ARG119 |
B | ASP224 |
B | ASP225 |
site_id | AC9 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE FAD C 998 |
Chain | Residue |
C | TYR272 |
C | SER285 |
C | THR286 |
C | LYS287 |
C | PHE288 |
C | SER289 |
C | LEU292 |
C | GLU325 |
C | ARG329 |
C | PHE332 |
C | PHE388 |
C | ASN391 |
C | ARG394 |
C | GLN395 |
C | LEU420 |
C | ASP422 |
C | TYR423 |
C | ASP424 |
C | ASN428 |
C | ASN431 |
C | TRP432 |
C | HOH2159 |
C | HOH2161 |
C | HOH2209 |
C | HOH2223 |
C | HOH2252 |
I | DT2 |
I | TCP3 |
site_id | BC1 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE MHF C 999 |
Chain | Residue |
C | LYS89 |
C | CYS146 |
C | SER147 |
C | GLU148 |
C | GLU149 |
C | ASN341 |
C | PHE344 |
C | HIS345 |
C | GLU417 |
C | TYR423 |
C | PRO425 |
C | TYR429 |
C | HOH2253 |
C | HOH2255 |
C | HOH2256 |
C | HOH2257 |
D | PHE188 |
D | ASP189 |
D | LYS338 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL C 1499 |
Chain | Residue |
C | ARG51 |
C | ASP54 |
C | ASP56 |
C | HIS142 |
C | ARG300 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL C 1500 |
Chain | Residue |
C | GLY281 |
C | HOH2142 |
C | HOH2243 |
site_id | BC4 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE FAD D 998 |
Chain | Residue |
D | TYR272 |
D | SER285 |
D | THR286 |
D | LYS287 |
D | PHE288 |
D | SER289 |
D | LEU292 |
D | GLU325 |
D | ARG329 |
D | PHE332 |
D | PHE388 |
D | ASN391 |
D | ARG394 |
D | GLN395 |
D | LEU420 |
D | ASP422 |
D | TYR423 |
D | ASP424 |
D | SER427 |
D | ASN428 |
D | ASN431 |
D | TRP432 |
D | HOH2143 |
D | HOH2144 |
D | HOH2190 |
D | HOH2200 |
D | HOH2205 |
J | DT2 |
J | TCP3 |
site_id | BC5 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE MHF D 999 |
Chain | Residue |
C | PHE188 |
C | ASP189 |
C | ASP192 |
C | LYS338 |
D | LYS89 |
D | CYS146 |
D | SER147 |
D | GLU148 |
D | GLU149 |
D | ASN341 |
D | PHE344 |
D | HIS345 |
D | GLU417 |
D | TYR423 |
D | PRO425 |
D | TYR429 |
D | HOH2206 |
D | HOH2208 |
D | HOH2209 |
site_id | BC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CL D 1498 |
Chain | Residue |
D | ARG51 |
D | ASP54 |
D | ASP56 |
D | HIS142 |
D | ARG300 |
D | HOH2160 |
site_id | BC7 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE FAD E 998 |
Chain | Residue |
E | TYR272 |
E | SER285 |
E | THR286 |
E | LYS287 |
E | PHE288 |
E | SER289 |
E | LEU292 |
E | GLU325 |
E | ARG329 |
E | PHE332 |
E | PHE388 |
E | ASN391 |
E | ARG394 |
E | GLN395 |
E | LEU420 |
E | ASP422 |
E | TYR423 |
E | ASP424 |
E | SER427 |
E | ASN428 |
E | ASN431 |
E | TRP432 |
E | HOH2146 |
E | HOH2147 |
E | HOH2197 |
E | HOH2211 |
E | HOH2230 |
K | DT2 |
K | TCP3 |
site_id | BC8 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE MHF E 999 |
Chain | Residue |
E | LYS89 |
E | CYS146 |
E | SER147 |
E | GLU148 |
E | GLU149 |
E | ASN341 |
E | PHE344 |
E | HIS345 |
E | GLU417 |
E | TYR423 |
E | PRO425 |
E | TYR429 |
E | HOH2231 |
E | HOH2233 |
F | PHE188 |
F | ASP189 |
F | LYS338 |
site_id | BC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL E 1499 |
Chain | Residue |
E | ARG51 |
E | ASP54 |
E | ASP56 |
E | HIS142 |
E | ARG300 |
site_id | CC1 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE FAD F 998 |
Chain | Residue |
F | TYR272 |
F | SER285 |
F | THR286 |
F | LYS287 |
F | PHE288 |
F | SER289 |
F | LEU292 |
F | GLU325 |
F | ARG329 |
F | PHE388 |
F | ASN391 |
F | ARG394 |
F | GLN395 |
F | LEU420 |
F | ASP422 |
F | TYR423 |
F | ASP424 |
F | SER427 |
F | ASN428 |
F | ASN431 |
F | TRP432 |
F | HOH2077 |
F | HOH2078 |
F | HOH2106 |
F | HOH2116 |
L | DT2 |
L | TCP3 |
site_id | CC2 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE MHF F 999 |
Chain | Residue |
E | PHE188 |
E | ASP189 |
E | ASP192 |
E | LYS338 |
E | HOH2107 |
F | HIS83 |
F | LYS89 |
F | CYS146 |
F | SER147 |
F | GLU148 |
F | GLU149 |
F | ASN341 |
F | PHE344 |
F | HIS345 |
F | GLU417 |
F | TYR423 |
F | PRO425 |
F | TYR429 |
F | HOH2119 |
site_id | CC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL F 1498 |
Chain | Residue |
F | HIS5 |
F | GLY281 |
F | HOH2068 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
B | TYR272 | |
C | ASP422 | |
C | ASP424 | |
C | ASP441 | |
D | TYR272 | |
D | SER285 | |
D | ARG392 | |
D | ASP422 | |
D | ASP424 | |
D | ASP441 | |
E | TYR272 | |
B | SER285 | |
E | SER285 | |
E | ARG392 | |
E | ASP422 | |
E | ASP424 | |
E | ASP441 | |
F | TYR272 | |
F | SER285 | |
F | ARG392 | |
F | ASP422 | |
F | ASP424 | |
B | ARG392 | |
F | ASP441 | |
B | ASP422 | |
B | ASP424 | |
B | ASP440 | |
C | TYR272 | |
C | SER285 | |
C | ARG392 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1dnp |
Chain | Residue | Details |
A | TRP356 | |
A | TRP432 | |
A | TRP409 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1dnp |
Chain | Residue | Details |
C | TRP356 | |
C | TRP432 | |
C | TRP409 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1dnp |
Chain | Residue | Details |
D | TRP356 | |
D | TRP432 | |
D | TRP409 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1dnp |
Chain | Residue | Details |
E | TRP356 | |
E | TRP432 | |
E | TRP409 |
site_id | CSA5 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1dnp |
Chain | Residue | Details |
F | TRP356 | |
F | TRP432 | |
F | TRP409 |
site_id | CSA6 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1dnp |
Chain | Residue | Details |
B | TRP356 | |
B | TRP432 | |
B | TRP409 |