Structure of PDB 2psj Chain A

Receptor sequence
>2psjA (length=306) Species: 6136 (Renilla reniformis) [Search protein sequence]
SKVYDPEQRKRMITGPQWWARCKQMNVLDSFINYYDSEKHAENAVIFLHG
NATSSYLWRHVVPHIEPVARCIIPDLIGMGKSGKSGNGSYRLLDHYKYLT
AWFELLNLPKKIIFVGHDWGAALAFHYAYEHQDRIKAIVHMESVVDVIES
EWPDIEEDIALIKSEEGEKMVLENNFFVETVLPSKIMRKLEPEEFAAYLE
PFKEKGEVRRPTLSWPREIPLVKGGKPDVVQIVRNYNAYLRASDDLPKLF
IESDPGFFSNAIVEGAKKFPNTEFVKVKGLHFLQEDAPDEMGKYIKSFVE
RVLKNE
3D structure
PDB2psj Crystal Structures of the Luciferase and Green Fluorescent Protein from Renilla reniformis.
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) N53 D120 W121 E144 W156 G260 H285
Catalytic site (residue number reindexed from 1) N51 D118 W119 E142 W152 G256 H281
Enzyme Commision number 1.13.12.5: Renilla-type 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 CEI A W156 D162 F180 K189 F261 H285 W152 D158 F176 K185 F257 H281 MOAD: Ki~20nM
PDBbind-CN: -logKd/Ki=7.70,Ki=20nM
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004301 epoxide hydrolase activity
GO:0004497 monooxygenase activity
GO:0016787 hydrolase activity
GO:0016831 carboxy-lyase activity
GO:0050248 Renilla-luciferin 2-monooxygenase activity
Biological Process
GO:0008218 bioluminescence

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Molecular Function
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Biological Process
External links
PDB RCSB:2psj, PDBe:2psj, PDBj:2psj
PDBsum2psj
PubMed17980388
UniProtP27652|LUCI_RENRE Coelenterazine h 2-monooxygenase

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