Structure of PDB 3kou Chain A

Receptor sequence
>3kouA (length=237) Species: 9913 (Bos taurus) [Search protein sequence]
RWHGAGSTADFQKIIQERCDTYTQTIRPGSRSRNCQAIRQAFMSAFISKD
PCKATKEDYNSLINLAPPTVPCGQQVFWSKTKELAHEYAKRRRLMTLEDT
LLGYLADGLRWCGEPGSSDLNIWSCPDWRKDCRTNYLSVFWEVLSERFAE
SACNTVRVVLNGSLENAFDSMSIFGRVEAPNLRPQVELEAWLVHDTGKPP
SDSCSGSSIRKLKSILDGRNVKFRCMDNLSRDQFLQR
3D structure
PDB3kou Insights into the mechanism of bovine CD38/NAD+glycohydrolase from the X-ray structures of its Michaelis complex and covalently-trapped intermediates.
ChainA
Resolution1.78 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E138 I213 E218
Catalytic site (residue number reindexed from 1) E98 I173 E178
Enzyme Commision number 2.4.99.20: 2'-phospho-ADP-ribosyl cyclase/2'-phospho-cyclic-ADP-ribose transferase.
3.2.2.6: ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase.
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 2NF A F117 W118 S119 K120 S185 F188 I213 F214 E218 F77 W78 S79 K80 S145 F148 I173 F174 E178
Gene Ontology
Molecular Function
GO:0016740 transferase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0061809 NAD+ nucleotidase, cyclic ADP-ribose generating
Cellular Component
GO:0016020 membrane

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Molecular Function
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Cellular Component
External links
PDB RCSB:3kou, PDBe:3kou, PDBj:3kou
PDBsum3kou
PubMed22529956
UniProtQ9TTF5

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