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 | 0006281 | biological_process | DNA repair |
| A | 0006974 | biological_process | DNA damage response |
| 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 |
| 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 | 0006281 | biological_process | DNA repair |
| B | 0006974 | biological_process | DNA damage response |
| 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 |
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 | 264 |
| Details | Domain: {"description":"Photolyase/cryptochrome alpha/beta"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | Region: {"description":"Interaction with DNA","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"7604260","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DNP","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 30 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"7604260","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | Site: {"description":"Electron transfer via tryptophanyl radical"} |
| Chain | Residue | Details |
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 |
