4LEZ: Mouse cGAS

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.

Method
X-ray diffraction
Resolution
2.36 Å
Organism
Mus musculus
Chains
6
Atoms
7,645
Mol. weight
109.51 kDa
Ligands
1SY, ZN
Released
25 Dec 2013

Explore 4LEZ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 20 helices, 15 β-strands

ElementResiduesLengthSheet
α-helix150-1578
α-helix158-1603
α-helix161-18222
β-strand193-19751
α-helix199-2024
β-strand211-21991
β-strand224-22741
β-strand234-23851
α-helix249-2513
β-strand25212
β-strand25611
β-strand25712
α-helix259-27517
β-strand281-28441
α-helix287-2882
β-strand293-30081
β-strand302-314131
α-helix317-3193
α-helix320-3223
α-helix334-3418
β-strand345-34951
α-helix359-3613
β-strand363-36641
α-helix368-3769
β-strand38113
α-helix394-41118
α-helix413-4153
α-helix420-43314
α-helix437-4404
α-helix442-4443
α-helix445-46218
β-strand46614
β-strand47414
α-helix483-49816
α-helix502-5054
Chain C: 19 helices, 15 β-strands
ElementResiduesLengthSheet
α-helix150-1578
α-helix161-18424
β-strand193-19755
α-helix199-2024
β-strand211-21995
β-strand223-22755
β-strand234-23965
β-strand25216
β-strand25615
β-strand25716
α-helix259-27517
β-strand281-28445
α-helix287-2882
β-strand293-29975
β-strand303-314125
α-helix317-3193
α-helix320-3223
α-helix334-3429
β-strand345-34845
α-helix350-3523
α-helix359-3613
β-strand363-36645
α-helix368-3769
β-strand38113
α-helix394-41118
α-helix413-4153
α-helix420-43314
α-helix437-4404
α-helix442-4443
α-helix445-46218
β-strand46617
β-strand47417
α-helix483-49816
α-helix502-5043

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Cyclic GMP-AMP synthaseA, Cprotein366Mus musculusQ8C6L5 (AlphaFold model)
18bp dsDNAE, F, I, JDNA18
Sequence of entity 1 (A, C), FASTA
>4LEZ_1 Cyclic GMP-AMP synthase (chains A, C)
GSRKEPDKLKKVLDKLRLKRKDISEAAETVNKVVERLLRRMQKRESEFKGVEQLNTGSYY
EHVKISAPNEFDVMFKLEVPRIELQEYYETGAFYLVKFKRIPRGNPLSHFLEGEVLSATK
MLSKFRKIIKEEVKEIKDIDVSVEKEKPGSPAVTLLIRNPEEISVDIILALESKGSWPIS
TKEGLPIQGWLGTKVRTNLRREPFYLVPKNAKDGNSFQGETWRLSFSHTEKYILNNHGIE
KTCCESSGAKCCRKECLKLMKYLLEQLKKEFQELDAFCSYHVKTAIFHMWTQDPQDSQWD
PRNLSSCFDKLLAFFLECLRTEKLDHYFIPKFNLFSQELIDRKSKEFLSKKIEYERNNGF
PIFDKL
Sequence of entity 2 (E, F, I, J), FASTA
>4LEZ_2 18bp dsDNA (chains E, F, I, J)
ATCTGTACATGTACAGAT

Ligands and cofactors

IDNameFormulaCopies
1SYcGAMPC20 H24 N10 O13 P22
ZNZinc ionZn2

Primary citation

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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