Structure of PDB 3rix Chain A

Receptor sequence
>3rixA (length=428) Species: 7054 (Photinus pyralis) [Search protein sequence]
DAKNIKKGPAPFYPLEDGTAGEQLHKAMKRYALVPGTIAFTDAHIEVNIT
YAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAV
APANDIYNERELLNSMNISQPTVVFVSKKGLQKILNVQKKLPIIQKIIIM
DSKTDYQGFQSMYTFVTSHLPPGFNEYDFVPESFDRDKTIALIMNSLPKG
VALPHRTACVRFSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLI
CGFRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLS
NLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETTSAILITPEGDD
KPGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEA
TNALIDKDGWLHSGDIAYWDEDEHFFIV
3D structure
PDB3rix Titration-based screening for evaluation of natural product extracts: identification of an aspulvinone family of luciferase inhibitors.
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S198 R218 H245 T343 E344
Catalytic site (residue number reindexed from 1) S196 R211 H238 T336 E337
Enzyme Commision number 1.13.12.7: firefly luciferase.
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 923 A R218 H245 F247 G315 G316 R337 Q338 G339 G341 L342 T343 S347 A348 R211 H238 F240 G308 G309 R330 Q331 G332 G334 L335 T336 S340 A341
Gene Ontology
Molecular Function
GO:0004467 long-chain fatty acid-CoA ligase activity
GO:0004497 monooxygenase activity
GO:0005524 ATP binding
GO:0046872 metal ion binding
GO:0047077 Photinus-luciferin 4-monooxygenase (ATP-hydrolyzing) activity
GO:0051087 protein-folding chaperone binding
Biological Process
GO:0001676 long-chain fatty acid metabolic process
GO:0008218 bioluminescence
GO:0046949 fatty-acyl-CoA biosynthetic process
Cellular Component
GO:0005777 peroxisome

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Biological Process
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Cellular Component
External links
PDB RCSB:3rix, PDBe:3rix, PDBj:3rix
PDBsum3rix
PubMed22118678
UniProtP08659|LUCI_PHOPY Luciferin 4-monooxygenase

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