Complex of GS-alpha with the catalytic domains of mammalian adenylyl cyclase: complex with MANT-ITP and Mn. Determined by X-ray diffraction at 3.11 Å resolution. Released 16 Feb 2010.
Explore 3G82 in 3D Show helices and sheets RCSB PDB PDBe
3G82 contains 30 α-helices and 27 β-strands across 3 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 383-398 | 16 | 1 |
| α-helix | 400-403 | 4 | |
| α-helix | 409-429 | 21 | |
| β-strand | 433-438 | 6 | 1 |
| β-strand | 441-446 | 6 | 1 |
| α-helix | 455-477 | 23 | |
| β-strand | 482-496 | 15 | 1 |
| β-strand | 505-507 | 3 | 1 |
| α-helix | 509-519 | 11 | |
| β-strand | 526-529 | 4 | 1 |
| α-helix | 530-534 | 5 | |
| β-strand | 544 | 1 | 1 |
| α-helix | 547-549 | 3 | |
| α-helix | 552-555 | 4 | |
| β-strand | 561-563 | 3 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 881-891 | 11 | 2 |
| α-helix | 894-898 | 5 | |
| α-helix | 909-923 | 15 | |
| β-strand | 934-940 | 7 | 2 |
| β-strand | 943-948 | 6 | 2 |
| α-helix | 967-990 | 24 | |
| β-strand | 997-1006 | 10 | 2 |
| β-strand | 1009-1010 | 2 | 3 |
| β-strand | 1016-1017 | 2 | 3 |
| β-strand | 1020 | 1 | 2 |
| α-helix | 1022-1032 | 11 | |
| β-strand | 1039-1042 | 4 | 2 |
| α-helix | 1043-1052 | 10 | |
| β-strand | 1056-1064 | 9 | 2 |
| β-strand | 1068-1075 | 8 | 2 |
| α-helix | 1076 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 40-47 | 8 | 4 |
| α-helix | 53-64 | 12 | |
| α-helix | 89-111 | 23 | |
| α-helix | 116-119 | 4 | |
| α-helix | 122-124 | 3 | |
| α-helix | 125-133 | 9 | |
| α-helix | 144-155 | 12 | |
| α-helix | 157-163 | 7 | |
| α-helix | 175-179 | 5 | |
| α-helix | 182-185 | 4 | |
| α-helix | 194-199 | 6 | |
| β-strand | 207-214 | 8 | 4 |
| β-strand | 217-224 | 8 | 4 |
| α-helix | 228-237 | 10 | |
| β-strand | 243-249 | 7 | 4 |
| α-helix | 252-254 | 3 | |
| β-strand | 256 | 1 | 5 |
| β-strand | 264 | 1 | 5 |
| α-helix | 265-277 | 13 | |
| β-strand | 286-292 | 7 | 4 |
| α-helix | 294-303 | 10 | |
| α-helix | 313-316 | 4 | |
| α-helix | 332-349 | 18 | |
| β-strand | 359-360 | 2 | 4 |
| β-strand | 363 | 1 | 4 |
| α-helix | 369-385 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Adenylate cyclase type 5 | A | protein | 225 | Canis lupus familiaris | P30803 (AlphaFold model) |
| Adenylate cyclase type 2 | B | protein | 212 | Rattus norvegicus | P26769 (AlphaFold model) |
| Guanine nucleotide-binding protein G(s) subunit alpha isoforms short | C | protein | 394 | Bos taurus | P04896 (AlphaFold model) |
>3G82_1 Adenylate cyclase type 5 (chains A) MHHHHHHAMEMKADINAKQEDMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMT LNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGMDMIEAISLVRE MTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLSY LNGDYEVEPGCGGERNAYLKEHSIETFLILRCTQKRKEEKAMIAK
>3G82_2 Adenylate cyclase type 2 (chains B) RSLKNEELYHQSYDCVCVMFASIPDFKEFYTESDVNKEGLECLRLLNEIIADFDDLLSKP KFSGVEKIKTIGSTYMAATGLSAIPSQEHAQEPERQYMHIGTMVEFAYALVGKLDAINKH SFNDFKLRVGINHGPVIAGVIGAQKPQYDIWGNTVNVASRMDSTGVLDKIQVTEETSLIL QTLGYTCTCRGIINVKGKGDLKTYFVNTEMSR
>3G82_3 Guanine nucleotide-binding protein G(s) subunit alpha isoforms short (chains C) MGCLGNSKTEDQRNEEKAQREANKKIEKQLQKDKQVYRATHRLLLLGAGESGKSTIVKQM RILHVNGFNGEGGEEDPQAARSNSDGEKATKVQDIKNNLKEAIETIVAAMSNLVPPVELA NPENQFRVDYILSVMNVPDFDFPPEFYEHAKALWEDEGVRACYERSNEYQLIDCAQYFLD KIDVIKQDDYVPSDQDLLRCRVLTSGIFETKFQVDKVNFHMFDVGGQRDERRKWIQCFND VTAIIFVVASSSYNMVIREDNQTNRLQEALNLFKSIWNNRWLRTISVILFLNKQDLLAEK VLAGKSKIEDYFPEFARYTTPEDATPEPGEDPRVTRAKYFIRDEFLRISTASGDGRHYCY PHFTCAVDTENIRRVFNDCRDIIQRMHLRQYELL
| ID | Name | Formula | Copies |
|---|---|---|---|
| GSP | 5'-guanosine-diphosphate-monothiophosphate | C10 H16 N5 O13 P3 S | 1 |
| MG | Magnesium ion | Mg | 1 |
| MI3 | 3'-O-{[2-(methylamino)phenyl]carbonyl}inosine 5'-(tetrahydrogen triphosphate) | C18 H22 N5 O15 P3 | 1 |
| FOK | Forskolin | C22 H34 O7 | 1 |
| MN | Manganese (II) ion | Mn | 2 |
Water and common crystallization additives (CL) are not listed.
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. Huebner, M., Geduhn, J., Pinto, C. et al. To be published.
Other PDB entries of the same protein (UniProt P30803 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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