Structure of PDB 1own Chain A

Receptor sequence
>1ownA (length=474) Species: 269084 (Synechococcus elongatus PCC 6301) [Search protein sequence]
AAPILFWHRRDLRLSDNIGLAAARAQSAQLIGLFCLDPQILQSADMAPAR
VAYLQGCLQELQQRYQQAGSRLLLLQGDPQHLIPQLAQQLQAEAVYWNQD
IEPYGRDRDGQVAAALKTAGIRAVQLWDQLLHSPDQILSGSGNPYSVYGP
FWKNWQAQPKPTPVATPTELVDLSPEQLTAIAPLLLSELPTLKQLGFDWD
GGFPVEPGETAAIARLQEFCDRAIADYDPQRNFPAEAGTSGLSPALKFGA
IGIRQAWQAASAAHALSRSDEARNSIRVWQQELAWREFYQHALYHFPSLA
DGPYRSLWQQFPWENREALFTAWTQAQTGYPIVDAAMRQLTETGWMHNRC
RMIVASFLTKDLIIDWRRGEQFFMQHLVDGDLAANNGGWQWSASSGMDPK
PLRIFNPASQAKKFDATATYIKRWLPELRHVHPKDLISGEITPIERRGYP
APIVNHNLRQKQFKALYNQLKAAI
3D structure
PDB1own DNA apophotolyase from Anacystis nidulans: 1.8 A structure, 8-HDF reconstitution and X-ray-induced FAD reduction.
ChainA
Resolution2.3 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) E282 W285 W313 N348 W366 W389
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
View graph for
Biological Process
External links
PDB RCSB:1own, PDBe:1own, PDBj:1own
PDBsum1own
PubMed15213381
UniProtP05327|PHR_SYNP6 Deoxyribodipyrimidine photo-lyase (Gene Name=phr)

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