Structure of PDB 1r15 Chain B

Receptor sequence
>1r15B (length=251) Species: 6500 (Aplysia californica) [Search protein sequence]
IVPTRELENVFLGRCKDYEITRYLDILPRVRSDCSALWKDFFKAFSFKNP
CDLDLGSYKDFFTSAQQQLPKNKVMFWSGVYDEAHDYANTGRKYITLEDT
LPGYMLNSLVWCGQRANPGFNEKVCPDFKTCPVQARESFWGMASSSYAHS
AEGEVTYMVDGSNPKVPAYRPDSFFGKYELPNLTNKVTRVKVIVLHRLGE
KIIEKCGAGSLLDLEKLVKAKHFAFDCVENPRAVLFLLCSDNPNARECRL
A
3D structure
PDB1r15 ADP-ribosyl cyclase; crystal structures reveal a covalent intermediate.
ChainB
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E98 F174 E179
Catalytic site (residue number reindexed from 1) E98 F174 E179
Enzyme Commision number 2.4.99.20: 2'-phospho-ADP-ribosyl cyclase/2'-phospho-cyclic-ADP-ribose transferase.
3.2.2.-
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 N B W77 S78 L97 S144 F174 E179 W77 S78 L97 S144 F174 E179
BS02 NCA B V110 W111 R136 W140 V110 W111 R136 W140
Gene Ontology
Molecular Function
GO:0003953 NAD+ nucleosidase activity
GO:0016740 transferase activity
GO:0016787 hydrolase activity
GO:0016849 phosphorus-oxygen lyase activity
GO:0061809 NAD+ nucleotidase, cyclic ADP-ribose generating
Biological Process
GO:0007338 single fertilization
GO:0030890 positive regulation of B cell proliferation
Cellular Component
GO:0005886 plasma membrane
GO:0016020 membrane
GO:0031410 cytoplasmic vesicle

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1r15, PDBe:1r15, PDBj:1r15
PDBsum1r15
PubMed15016363
UniProtP29241|NADA_APLCA ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase

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