Structure of PDB 6c7o Chain A

Receptor sequence
>6c7oA (length=479) Species: 1111708 (Synechocystis sp. PCC 6803 substr. Kazusa) [Search protein sequence]
QRSYSPQDWLRGYQSQPQEWDYWVEDVEGSIPLWLQGTLYRNGPGLLEIG
DRPLKHPFDGDGMVTAFKFPGDGRVHFQSKFVRTQGYVEEQKAGKMIYRG
VFGSQPAGGWLKTIFDLRLKNIANTNITYWGDRLLALWEGGQPHRLEPSN
LATIGLDDLGGILAEGQPLSAHPRIDPASTFDGGQPCYVTFSIKSSLSST
LTLLELDPQGKLLRQKTETFPGFAFIHDFAITPHYAIFLQNNVTLNGLPY
LFGLRGAGECVQFHPDKPAQIILVPRDGGEIKRIPVQAGFVFHHANAFEE
NGKIILDSICYNSLPQVDTDGDFRSTNFDNLDPGQLWRFTIDPAAATVEK
QLMVSRCCEFPVVHPQQVGRPYRYVYMGAAHHSTGNAPLQAILKVDLESG
TETLRSFAPHGFAGEPIFVSHPGALEEDDGVLLCLIYKADLHRSELVILN
AKDITAPAIATLKLKHHIPYPLHGSWAQT
3D structure
PDB6c7o Insights into the pathogenesis of dominant retinitis pigmentosa associated with a D477G mutation in RPE65.
ChainA
Resolution3.15 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.13.11.75: all-trans-8'-apo-beta-carotenal 15,15'-oxygenase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 FE2 A H183 H238 H304 H484 H172 H227 H293 H473
Gene Ontology
Molecular Function
GO:0010436 carotenoid dioxygenase activity
GO:0016702 oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity
GO:0102162 all-trans-8'-apo-beta-carotenal 15,15'-oxygenase activity
Biological Process
GO:0016121 carotene catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:6c7o, PDBe:6c7o, PDBj:6c7o
PDBsum6c7o
PubMed29659842
UniProtP74334|ACOX_SYNY3 Apocarotenoid-15,15'-oxygenase (Gene Name=sll1541)

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