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3I9K

Crystal structure of ADP ribosyl cyclase complexed with substrate NAD

Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
A0016020cellular_componentmembrane
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016849molecular_functionphosphorus-oxygen lyase activity
A0031410cellular_componentcytoplasmic vesicle
A0061809molecular_functionNAD+ nucleosidase activity, cyclic ADP-ribose generating
B0005886cellular_componentplasma membrane
B0016020cellular_componentmembrane
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0016849molecular_functionphosphorus-oxygen lyase activity
B0031410cellular_componentcytoplasmic vesicle
B0061809molecular_functionNAD+ nucleosidase activity, cyclic ADP-ribose generating
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE NAD B 301
ChainResidue
BPHE76
BSER144
BARG170
BSER173
BPHE174
BPHE175
BHOH263
BHOH275
BHOH280
BHOH331
BHOH344
BTRP77
BHOH352
BSER78
BGLY79
BLEU97
BGLU98
BASN107
BLYS129
BTRP140

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1r16
ChainResidueDetails
AGLU98
AGLY179

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1r16
ChainResidueDetails
BGLU98
BGLY179

site_idMCSA1
Number of Residues3
DetailsM-CSA 607
ChainResidueDetails
AGLU98electrostatic stabiliser
APHE174hydrophobic interaction
AGLY179covalent catalysis, covalently attached, nucleophile

site_idMCSA2
Number of Residues3
DetailsM-CSA 607
ChainResidueDetails
BGLU98electrostatic stabiliser
BPHE174hydrophobic interaction
BGLY179covalent catalysis, covalently attached, nucleophile

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PDB entries from 2026-04-01

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