Structure of PDB 5kjd Chain B

Receptor sequence
>5kjdB (length=479) Species: 1111708 (Synechocystis sp. PCC 6803 substr. Kazusa) [Search protein sequence]
QRSYSPQDWLRGYQSQPQEWDYWVEDVEGSIPPDLQGTLYRNGPGLLEIG
DRPLKHPFDGDGMVTAFKFPGDGRVHFQSKFVRTQGYVEEQKAGKMIYRG
VFGSQPAGGWLKTIFDLRLKNIANTNITYWGDRLLALWQGGQPHRLEPSN
LATIGLDDLGGILAEGQPLSAHPRIDPASTFDGGQPCYVTFSIKSSLSST
LTLLELDPQGKLLRQKTETFPGFAFIHDFAITPHYAIFLQNNVTLNGLPY
LFGLRGAGECVQFHPDKPAQIILVPRDGGEIKRIPVQAGFVFHHANAFEE
NGKIILDSICYNSLPQVDTDGDFRSTNFDNLDPGQLWRFTIDPAAATVEK
QLMVSRCCEFPVVHPQQVGRPYRYVYMGAAHHSTGNAPLQAILKVDLESG
TETLRSFAPHGFAGEPIFVPRPGGVAEDDGWLLCLIYKADLHRSELVILD
AQDITAPAIATLKLKHHIPYPLHGSWAQT
3D structure
PDB5kjd Key Residues for Catalytic Function and Metal Coordination in a Carotenoid Cleavage Dioxygenase.
ChainB
Resolution2.75 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 B 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:5kjd, PDBe:5kjd, PDBj:5kjd
PDBsum5kjd
PubMed27453555
UniProtP74334|ACOX_SYNY3 Apocarotenoid-15,15'-oxygenase (Gene Name=sll1541)

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