Complex Of Gs- With The Catalytic Domains Of Mammalian Adenylyl Cyclase: Complex With TNP-ATP and Mn. Determined by X-ray diffraction at 2.9 Å resolution. Released 4 Jul 2006.
Explore 2GVD in 3D Show helices and sheets RCSB PDB PDBe
2GVD contains 32 α-helices and 31 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 | 397 | 1 | 2 |
| α-helix | 401-404 | 4 | |
| α-helix | 409-429 | 21 | |
| β-strand | 432-438 | 7 | 1 |
| β-strand | 441-446 | 6 | 1 |
| α-helix | 455-476 | 22 | |
| β-strand | 483 | 1 | 2 |
| β-strand | 484-496 | 13 | 1 |
| β-strand | 505-507 | 3 | 1 |
| α-helix | 509-519 | 11 | |
| β-strand | 525-528 | 4 | 1 |
| α-helix | 530-534 | 5 | |
| β-strand | 544 | 1 | 1 |
| α-helix | 547-549 | 3 | |
| α-helix | 552-556 | 5 | |
| β-strand | 562-563 | 2 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 881 | 1 | 3 |
| β-strand | 885-891 | 7 | 4 |
| α-helix | 895-898 | 4 | |
| α-helix | 909-923 | 15 | |
| α-helix | 929-931 | 3 | |
| β-strand | 934-940 | 7 | 4 |
| β-strand | 943-948 | 6 | 4 |
| α-helix | 967-990 | 24 | |
| β-strand | 997-1003 | 7 | 4 |
| β-strand | 1006-1010 | 5 | 3 |
| β-strand | 1016-1020 | 5 | 3 |
| α-helix | 1022-1032 | 11 | |
| β-strand | 1038-1042 | 5 | 4 |
| α-helix | 1043-1051 | 9 | |
| β-strand | 1056-1064 | 9 | 4 |
| β-strand | 1068-1075 | 8 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 40 | 1 | 5 |
| β-strand | 43-47 | 5 | 6 |
| α-helix | 53-63 | 11 | |
| α-helix | 89-108 | 20 | |
| α-helix | 116-117 | 2 | |
| α-helix | 122-124 | 3 | |
| α-helix | 125-133 | 9 | |
| α-helix | 144-155 | 12 | |
| α-helix | 157-163 | 7 | |
| α-helix | 166-168 | 3 | |
| α-helix | 175-180 | 6 | |
| α-helix | 182-185 | 4 | |
| α-helix | 194-199 | 6 | |
| β-strand | 208-210 | 3 | 6 |
| β-strand | 213 | 1 | 5 |
| β-strand | 218 | 1 | 5 |
| β-strand | 221-223 | 3 | 6 |
| α-helix | 230-237 | 8 | |
| β-strand | 243-247 | 5 | 6 |
| β-strand | 256 | 1 | 7 |
| β-strand | 264 | 1 | 7 |
| α-helix | 265-277 | 13 | |
| β-strand | 287-291 | 5 | 6 |
| α-helix | 294-303 | 10 | |
| α-helix | 308-310 | 3 | |
| α-helix | 313-316 | 4 | |
| α-helix | 326-327 | 2 | |
| α-helix | 332-350 | 19 | |
| β-strand | 359-363 | 5 | 6 |
| α-helix | 369-380 | 12 |
| 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) |
>2GVD_1 Adenylate cyclase type 5 (chains A) MHHHHHHAMEMKADINAKQEDMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMT LNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGMDMIEAISLVRE MTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLSY LNGDYEVEPGCGGERNAYLKEHSIETFLILRCTQKRKEEKAMIAK
>2GVD_2 Adenylate cyclase type 2 (chains B) RSLKNEELYHQSYDCVCVMFASIPDFKEFYTESDVNKEGLECLRLLNEIIADFDDLLSKP KFSGVEKIKTIGSTYMAATGLSAIPSQEHAQEPERQYMHIGTMVEFAYALVGKLDAINKH SFNDFKLRVGINHGPVIAGVIGAQKPQYDIWGNTVNVASRMDSTGVLDKIQVTEETSLIL QTLGYTCTCRGIINVKGKGDLKTYFVNTEMSR
>2GVD_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 |
| 128 | SPIRO(2,4,6-TRINITROBENZENE[1,2A]-2O',3O'-methylene-adenine-triphosphate | C16 H16 N8 O19 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 2GVD 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.