1DNP
STRUCTURE OF DEOXYRIBODIPYRIMIDINE PHOTOLYASE
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 | 0003684 | molecular_function | damaged DNA binding |
A | 0003904 | molecular_function | deoxyribodipyrimidine photo-lyase activity |
A | 0005515 | molecular_function | protein binding |
A | 0006139 | biological_process | nucleobase-containing compound metabolic process |
A | 0006281 | biological_process | DNA repair |
A | 0006950 | biological_process | response to stress |
A | 0007603 | biological_process | phototransduction, visible light |
A | 0009416 | biological_process | response to light stimulus |
A | 0016829 | molecular_function | lyase activity |
A | 0071949 | molecular_function | FAD binding |
A | 0097159 | molecular_function | organic cyclic compound binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0000719 | biological_process | photoreactive repair |
B | 0003677 | molecular_function | DNA binding |
B | 0003684 | molecular_function | damaged DNA binding |
B | 0003904 | molecular_function | deoxyribodipyrimidine photo-lyase activity |
B | 0005515 | molecular_function | protein binding |
B | 0006139 | biological_process | nucleobase-containing compound metabolic process |
B | 0006281 | biological_process | DNA repair |
B | 0006950 | biological_process | response to stress |
B | 0007603 | biological_process | phototransduction, visible light |
B | 0009416 | biological_process | response to light stimulus |
B | 0016829 | molecular_function | lyase activity |
B | 0071949 | molecular_function | FAD binding |
B | 0097159 | molecular_function | organic cyclic compound binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE FAD A 472 |
Chain | Residue |
A | TYR222 |
A | TYR281 |
A | TRP338 |
A | ASN341 |
A | ARG344 |
A | LEU370 |
A | ASP372 |
A | GLY373 |
A | ASP374 |
A | ALA377 |
A | ASN378 |
A | THR234 |
A | GLY381 |
A | TRP382 |
A | HOH514 |
A | HOH526 |
A | HOH617 |
A | HOH704 |
A | HOH747 |
A | HOH835 |
A | SER235 |
A | ARG236 |
A | LEU237 |
A | SER238 |
A | TRP271 |
A | GLU274 |
A | ARG278 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MHF A 473 |
Chain | Residue |
A | HIS44 |
A | GLU106 |
A | ASN108 |
A | GLU109 |
A | CYS292 |
A | LYS293 |
site_id | AC3 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE FAD B 472 |
Chain | Residue |
B | TYR222 |
B | THR234 |
B | SER235 |
B | ARG236 |
B | LEU237 |
B | SER238 |
B | TRP271 |
B | GLU274 |
B | ARG278 |
B | TYR281 |
B | TRP338 |
B | ASN341 |
B | ARG344 |
B | LEU370 |
B | ASP372 |
B | GLY373 |
B | ASP374 |
B | ALA377 |
B | ASN378 |
B | GLY381 |
B | HOH511 |
B | HOH553 |
B | HOH596 |
B | HOH689 |
B | HOH797 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE MHF B 473 |
Chain | Residue |
B | HIS44 |
B | GLU106 |
B | ASN108 |
B | GLU109 |
B | CYS292 |
B | LYS293 |
B | GLY441 |
B | THR443 |
B | HOH813 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:7604260, ECO:0007744|PDB:1DNP |
Chain | Residue | Details |
A | ASN108 | |
A | GLU109 | |
B | ASN108 | |
B | GLU109 |
site_id | SWS_FT_FI2 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000269|PubMed:7604260 |
Chain | Residue | Details |
A | TYR222 | |
B | ASP372 | |
A | THR234 | |
A | TRP271 | |
A | GLU274 | |
A | ASP372 | |
B | TYR222 | |
B | THR234 | |
B | TRP271 | |
B | GLU274 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | ARG226 | |
A | GLN404 | |
B | ARG226 | |
B | GLN404 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | SITE: Electron transfer via tryptophanyl radical |
Chain | Residue | Details |
A | TRP306 | |
A | TRP359 | |
A | TRP382 | |
B | TRP306 | |
B | TRP359 | |
B | TRP382 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | a catalytic site defined by CSA, PubMed 7604260, 9360600 |
Chain | Residue | Details |
A | TRP306 | |
A | TRP359 | |
A | TRP382 |
site_id | CSA2 |
Number of Residues | 3 |
Details | a catalytic site defined by CSA, PubMed 7604260, 9360600 |
Chain | Residue | Details |
B | TRP306 | |
B | TRP359 | |
B | TRP382 |
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 183 |
Chain | Residue | Details |
A | GLU274 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | TRP277 | electron tunneling medium, polar/non-polar interaction, single electron acceptor, single electron donor, single electron relay, van der waals interaction |
A | TRP306 | single electron acceptor, single electron donor, single electron relay |
A | ASN341 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
A | TRP359 | single electron acceptor, single electron donor, single electron relay |
A | TRP382 | single electron acceptor, single electron donor, single electron relay |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 183 |
Chain | Residue | Details |
B | GLU274 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | TRP277 | electron tunneling medium, polar/non-polar interaction, single electron acceptor, single electron donor, single electron relay, van der waals interaction |
B | TRP306 | single electron acceptor, single electron donor, single electron relay |
B | ASN341 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
B | TRP359 | single electron acceptor, single electron donor, single electron relay |
B | TRP382 | single electron acceptor, single electron donor, single electron relay |