Crystal Structure of Complex of Gs- with The Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with MANT-ATP and Mn. Determined by X-ray diffraction at 3.27 Å resolution. Released 4 Jul 2006.
Explore 2GVZ in 3D Show helices and sheets RCSB PDB PDBe
2GVZ contains 28 α-helices and 30 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 | 383-396 | 14 | 1 |
| β-strand | 398 | 1 | 2 |
| α-helix | 400-404 | 5 | |
| α-helix | 409-429 | 21 | |
| β-strand | 432-438 | 7 | 1 |
| β-strand | 441-446 | 6 | 1 |
| α-helix | 455-468 | 14 | |
| β-strand | 482 | 1 | 2 |
| β-strand | 486-496 | 11 | 1 |
| β-strand | 505-506 | 2 | 1 |
| α-helix | 509-518 | 10 | |
| β-strand | 527-529 | 3 | 1 |
| α-helix | 530-533 | 4 | |
| β-strand | 542-544 | 3 | 1 |
| α-helix | 552-556 | 5 | |
| β-strand | 561-564 | 4 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 886-891 | 6 | 3 |
| α-helix | 893-898 | 6 | |
| α-helix | 912-923 | 12 | |
| β-strand | 934-940 | 7 | 3 |
| β-strand | 943-948 | 6 | 3 |
| α-helix | 968-987 | 20 | |
| β-strand | 997-1001 | 5 | 3 |
| β-strand | 1006-1010 | 5 | 4 |
| β-strand | 1016-1020 | 5 | 4 |
| α-helix | 1022-1029 | 8 | |
| β-strand | 1039 | 1 | 3 |
| β-strand | 1040-1042 | 3 | 5 |
| α-helix | 1043-1050 | 8 | |
| β-strand | 1056-1064 | 9 | 5 |
| β-strand | 1068-1075 | 8 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 40-47 | 8 | 6 |
| α-helix | 54-64 | 11 | |
| α-helix | 87-89 | 3 | |
| α-helix | 92-112 | 21 | |
| α-helix | 122-124 | 3 | |
| α-helix | 125-131 | 7 | |
| α-helix | 144-155 | 12 | |
| α-helix | 157-163 | 7 | |
| α-helix | 175-179 | 5 | |
| α-helix | 182-186 | 5 | |
| α-helix | 196-199 | 4 | |
| β-strand | 207-214 | 8 | 6 |
| β-strand | 217-224 | 8 | 6 |
| α-helix | 231-236 | 6 | |
| β-strand | 243-249 | 7 | 6 |
| α-helix | 252-254 | 3 | |
| β-strand | 256 | 1 | 7 |
| β-strand | 264 | 1 | 7 |
| α-helix | 265-277 | 13 | |
| β-strand | 286-287 | 2 | 6 |
| β-strand | 290-292 | 3 | 6 |
| α-helix | 294-303 | 10 | |
| α-helix | 313-315 | 3 | |
| α-helix | 332-351 | 20 | |
| β-strand | 359 | 1 | 6 |
| β-strand | 363 | 1 | 6 |
| 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), alpha subunit | C | protein | 394 | Bos taurus | P04896 (AlphaFold model) |
>2GVZ_1 Adenylate cyclase type 5 (chains A) MHHHHHHAMEMKADINAKQEDMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMT LNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGMDMIEAISLVRE MTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLSY LNGDYEVEPGCGGERNAYLKEHSIETFLILRCTQKRKEEKAMIAK
>2GVZ_2 Adenylate cyclase type 2 (chains B) RSLKNEELYHQSYDCVCVMFASIPDFKEFYTESDVNKEGLECLRLLNEIIADFDDLLSKP KFSGVEKIKTIGSTYMAATGLSAIPSQEHAQEPERQYMHIGTMVEFAYALVGKLDAINKH SFNDFKLRVGINHGPVIAGVIGAQKPQYDIWGNTVNVASRMDSTGVLDKIQVTEETSLIL QTLGYTCTCRGIINVKGKGDLKTYFVNTEMSR
>2GVZ_3 Guanine nucleotide-binding protein G(s), alpha subunit (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 |
| ONA | 3'-O-[2-(methylamino)benzoyl]adenosine 5'-(tetrahydrogen triphosphate) | C18 H23 N6 O14 P3 | 1 |
| FKP | Methylpiperazinoforskolin | C30 H50 N2 O7 | 1 |
| MN | Manganese (II) ion | Mn | 3 |
Water and common crystallization additives (CL) are not listed.
Broad specificity of Mammalian adenylyl cyclase for interaction with 2',3'-substituted purine- and pyrimidine nucleotide inhibitors. Mou, T.-C., Gille, A., Suryanarayana, S. et al. Mol Pharmacol (2006) 70:878-886. DOI 10.1124/mol.106.026427 · PubMed
Other PDB entries of the same protein (UniProt P30803 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 2GVZ directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.