Structure of PDB 1ism Chain A

Receptor sequence
>1ismA (length=250) Species: 9606 (Homo sapiens) [Search protein sequence]
WRAEGTSAHLRDIFLGRCAEYRALLSPEQRNKDCTAIWEAFKVALDKDPC
SVLPSDYDLFITLSRHSIPRDKSLFWENSHLLVNSFADNTRRFMPLSDVL
YGRVADFLSWCRQKADSGLDYQSCPTSEDCENNPVDSFWKRASIQYSKDS
SGVIHVMLNGSEPTGAYPIKGFFADYEIPNLQKEKITRIEIWVMHEIGGP
NVESCGEGSMKVLEKRLKDMGFQYSCINDYRPVKLLQCVDHSTHPDCALK
3D structure
PDB1ism Crystallographic studies on human BST-1/CD157 with ADP-ribosyl cyclase and NAD glycohydrolase activities.
ChainA
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S98 F173 E178
Catalytic site (residue number reindexed from 1) S97 F172 E177
Enzyme Commision number 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 NCA A W77 H81 L97 W140 F173 W76 H80 L96 W139 F172
Gene Ontology
Molecular Function
GO:0003953 NAD+ nucleosidase activity
GO:0016740 transferase activity
GO:0016787 hydrolase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0016849 phosphorus-oxygen lyase activity
GO:0061809 NAD+ nucleotidase, cyclic ADP-ribose generating
Biological Process
GO:0001952 regulation of cell-matrix adhesion
GO:0002691 regulation of cellular extravasation
GO:0006959 humoral immune response
GO:0007165 signal transduction
GO:0008284 positive regulation of cell population proliferation
GO:0030890 positive regulation of B cell proliferation
GO:0032956 regulation of actin cytoskeleton organization
GO:0050727 regulation of inflammatory response
GO:0050730 regulation of peptidyl-tyrosine phosphorylation
GO:0050848 regulation of calcium-mediated signaling
GO:0090022 regulation of neutrophil chemotaxis
GO:0090322 regulation of superoxide metabolic process
GO:2001044 regulation of integrin-mediated signaling pathway
Cellular Component
GO:0001931 uropod
GO:0005576 extracellular region
GO:0005886 plasma membrane
GO:0016020 membrane
GO:0035579 specific granule membrane
GO:0070062 extracellular exosome
GO:0098552 side of membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1ism, PDBe:1ism, PDBj:1ism
PDBsum1ism
PubMed11866528
UniProtQ10588|BST1_HUMAN ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2 (Gene Name=BST1)

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