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3G82

Complex of GS-alpha with the catalytic domains of mammalian adenylyl cyclase: complex with MANT-ITP and Mn

Summary for 3G82
Entry DOI10.2210/pdb3g82/pdb
Related1TL7 2GVD 2GVZ
DescriptorAdenylate cyclase type 5, Adenylate cyclase type 2, Guanine nucleotide-binding protein G(s) subunit alpha isoforms short, ... (10 entities in total)
Functional Keywordsadenylyl cyclase, mant-itp, alternative splicing, camp biosynthesis, glycoprotein, lyase, magnesium, membrane, metal-binding, phosphoprotein, transmembrane, cell membrane, gtp-binding, lipoprotein, nucleotide-binding, palmitate, transducer, lyase-lyase inhibitor complex, lyase/lyase inhibitor
Biological sourceCanis lupus familiaris (dogs)
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Cellular locationMembrane; Multi-pass membrane protein: P30803 P26769
Cell membrane; Lipid-anchor (By similarity): P04896
Total number of polymer chains3
Total formula weight96773.77
Authors
Huebner, M.,Mou, T.-C.,Sprang, S.R.,Seifert, R. (deposition date: 2009-02-11, release date: 2010-02-16, Last modification date: 2023-09-06)
Primary citationHuebner, M.,Geduhn, J.,Pinto, C.,Mou, T.-C.,Konig, B.,Sprang, S.R.,Seifert, R.
2',3'-(O)-(N-Methyl)anthraniloyl-inosine 5'-triphosphate is the Most Potent Adenylyl Cyclase 1 and 5 Inhibitor Known so far and Effectively Promotes Catalytic Subunit Assembly in the Absence of Forskolin
To be Published,
Experimental method
X-RAY DIFFRACTION (3.11 Å)
Structure validation

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