Structure of PDB 3i9j Chain B

Receptor sequence

>3i9jB (length=251) Species: 6500 (Aplysia californica)

IVPTRELENVFLGRCKDYEITRYLDILPRVRSDCSALWKDFFKAFSFKNP
CDLDLGSYKDFFTSAQQQLPKNKVMFWSGVYDEAHDYANTGRKYITLEDT
LPGYMLNSLVWCGQRANPGFNEKVCPDFKTCPVQARESFWGMASSSYAHS
AEGEVTYMVDGSNPKVPAYRPDSFFGKYELPNLTNKVTRVKVIVLHRLGE
KIIEKCGAGSLLDLEKLVKAKHFAFDCVENPRAVLFLLCSDNPNARECRL
A

3D structure

• PDB: 3i9j Structural basis for enzymatic evolution from a dedicated ADP-ribosyl cyclase to a multifunctional NAD hydrolase
• Chain: B
• Resolution: 2.18 Å

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	AVV	B	F76 W77 S78 G79 W140 F174 E179	F76 W77 S78 G79 W140 F174 E179
BS02	NCA	B	E98 W140 F174	E98 W140 F174

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

External links

• PDB: RCSB:3i9j, PDBe:3i9j, PDBj:3i9j
• PDBsum: 3i9j
• PubMed: 19640846
• UniProt: P29241|NADA_APLCA ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase