Structure of PDB 1qnf Chain A

Receptor sequence
>1qnfA (length=475) Species: 269084 (Synechococcus elongatus PCC 6301) [Search protein sequence]
MAAPILFWHRRDLRLSDNIGLAAARAQSAQLIGLFCLDPQILQSADMAPA
RVAYLQGCLQELQQRYQQAGSRLLLLQGDPQHLIPQLAQQLQAEAVYWNQ
DIEPYGRDRDGQVAAALKTAGIRAVQLWDQLLHSPDQILSGSGNPYSVYG
PFWKNWQAQPKPTPVATPTELVDLSPEQLTAIAPLLLSELPTLKQLGFDW
DGGFPVEPGETAAIARLQEFCDRAIADYDPQRNFPAEAGTSGLSPALKFG
AIGIRQAWQAASAAHALSRSDEARNSIRVWQQELAWREFYQHALYHFPSL
ADGPYRSLWQQFPWENREALFTAWTQAQTGYPIVDAAMRQLTETGWMHNR
CRMIVASFLTKDLIIDWRRGEQFFMQHLVDGDLAANNGGWQWSASSGMDP
KPLRIFNPASQAKKFDATATYIKRWLPELRHVHPKDLISGEITPIERRGY
PAPIVNHNLRQKQFKALYNQLKAAI
3D structure
PDB1qnf Crystal structure of DNA photolyase from Anacystis nidulans
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E283 W286 W314 N349 W367 W390
Catalytic site (residue number reindexed from 1) E283 W286 W314 N349 W367 W390
Enzyme Commision number 4.1.99.3: deoxyribodipyrimidine photo-lyase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003677 DNA binding
GO:0003904 deoxyribodipyrimidine photo-lyase activity
GO:0016829 lyase activity
GO:0071949 FAD binding
GO:0097159 organic cyclic compound binding
Biological Process
GO:0006139 nucleobase-containing compound metabolic process
GO:0006281 DNA repair
GO:0006950 response to stress
GO:0009416 response to light stimulus

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Molecular Function
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Biological Process
External links
PDB RCSB:1qnf, PDBe:1qnf, PDBj:1qnf
PDBsum1qnf
PubMed9360600
UniProtP05327|PHR_SYNP6 Deoxyribodipyrimidine photo-lyase (Gene Name=phr)

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