Structure of mouse cGAS bound to an 18bp DNA and cGAS product. Determined by X-ray diffraction at 2.36 Å resolution. Released 25 Dec 2013.
Explore 4LEZ in 3D Show helices and sheets RCSB PDB PDBe
4LEZ contains 39 α-helices and 30 β-strands across 2 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 |
|---|---|---|---|
| α-helix | 150-157 | 8 | |
| α-helix | 158-160 | 3 | |
| α-helix | 161-182 | 22 | |
| β-strand | 193-197 | 5 | 1 |
| α-helix | 199-202 | 4 | |
| β-strand | 211-219 | 9 | 1 |
| β-strand | 224-227 | 4 | 1 |
| β-strand | 234-238 | 5 | 1 |
| α-helix | 249-251 | 3 | |
| β-strand | 252 | 1 | 2 |
| β-strand | 256 | 1 | 1 |
| β-strand | 257 | 1 | 2 |
| α-helix | 259-275 | 17 | |
| β-strand | 281-284 | 4 | 1 |
| α-helix | 287-288 | 2 | |
| β-strand | 293-300 | 8 | 1 |
| β-strand | 302-314 | 13 | 1 |
| α-helix | 317-319 | 3 | |
| α-helix | 320-322 | 3 | |
| α-helix | 334-341 | 8 | |
| β-strand | 345-349 | 5 | 1 |
| α-helix | 359-361 | 3 | |
| β-strand | 363-366 | 4 | 1 |
| α-helix | 368-376 | 9 | |
| β-strand | 381 | 1 | 3 |
| α-helix | 394-411 | 18 | |
| α-helix | 413-415 | 3 | |
| α-helix | 420-433 | 14 | |
| α-helix | 437-440 | 4 | |
| α-helix | 442-444 | 3 | |
| α-helix | 445-462 | 18 | |
| β-strand | 466 | 1 | 4 |
| β-strand | 474 | 1 | 4 |
| α-helix | 483-498 | 16 | |
| α-helix | 502-505 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 150-157 | 8 | |
| α-helix | 161-184 | 24 | |
| β-strand | 193-197 | 5 | 5 |
| α-helix | 199-202 | 4 | |
| β-strand | 211-219 | 9 | 5 |
| β-strand | 223-227 | 5 | 5 |
| β-strand | 234-239 | 6 | 5 |
| β-strand | 252 | 1 | 6 |
| β-strand | 256 | 1 | 5 |
| β-strand | 257 | 1 | 6 |
| α-helix | 259-275 | 17 | |
| β-strand | 281-284 | 4 | 5 |
| α-helix | 287-288 | 2 | |
| β-strand | 293-299 | 7 | 5 |
| β-strand | 303-314 | 12 | 5 |
| α-helix | 317-319 | 3 | |
| α-helix | 320-322 | 3 | |
| α-helix | 334-342 | 9 | |
| β-strand | 345-348 | 4 | 5 |
| α-helix | 350-352 | 3 | |
| α-helix | 359-361 | 3 | |
| β-strand | 363-366 | 4 | 5 |
| α-helix | 368-376 | 9 | |
| β-strand | 381 | 1 | 3 |
| α-helix | 394-411 | 18 | |
| α-helix | 413-415 | 3 | |
| α-helix | 420-433 | 14 | |
| α-helix | 437-440 | 4 | |
| α-helix | 442-444 | 3 | |
| α-helix | 445-462 | 18 | |
| β-strand | 466 | 1 | 7 |
| β-strand | 474 | 1 | 7 |
| α-helix | 483-498 | 16 | |
| α-helix | 502-504 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cyclic GMP-AMP synthase | A, C | protein | 366 | Mus musculus | Q8C6L5 (AlphaFold model) |
| 18bp dsDNA | E, F, I, J | DNA | 18 |
>4LEZ_1 Cyclic GMP-AMP synthase (chains A, C) GSRKEPDKLKKVLDKLRLKRKDISEAAETVNKVVERLLRRMQKRESEFKGVEQLNTGSYY EHVKISAPNEFDVMFKLEVPRIELQEYYETGAFYLVKFKRIPRGNPLSHFLEGEVLSATK MLSKFRKIIKEEVKEIKDIDVSVEKEKPGSPAVTLLIRNPEEISVDIILALESKGSWPIS TKEGLPIQGWLGTKVRTNLRREPFYLVPKNAKDGNSFQGETWRLSFSHTEKYILNNHGIE KTCCESSGAKCCRKECLKLMKYLLEQLKKEFQELDAFCSYHVKTAIFHMWTQDPQDSQWD PRNLSSCFDKLLAFFLECLRTEKLDHYFIPKFNLFSQELIDRKSKEFLSKKIEYERNNGF PIFDKL
>4LEZ_2 18bp dsDNA (chains E, F, I, J) ATCTGTACATGTACAGAT
Cyclic GMP-AMP Synthase Is Activated by Double-Stranded DNA-Induced Oligomerization. Li, X., Shu, C., Yi, G. et al. Immunity (2013) 39:1019-1031. DOI 10.1016/j.immuni.2013.10.019 · PubMed
Other PDB entries of the same protein (UniProt Q8C6L5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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