4O6A: Mouse cyclic GMP-AMP synthase

Mouse cyclic GMP-AMP synthase (cGAS) in complex with DNA. Determined by X-ray diffraction at 1.86 Å resolution. Released 5 Feb 2014.

Method: X-ray diffraction
Resolution: 1.86 Å
Organism: Mus musculus
Chains: 6
Atoms: 8,279
Mol. weight: 106.07 kDa
Ligands: ZN
Released: 5 Feb 2014

Explore 4O6A in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4O6A contains 39 α-helices and 29 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: 19 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	147-157	11
α-helix	159-160	2
α-helix	161-184	24
β-strand	193-197	5	1
β-strand	211-219	9	1
β-strand	223-227	5	1
β-strand	234-239	6	1
α-helix	249-251	3
β-strand	252	1	2
β-strand	256	1	1
β-strand	257	1	2
α-helix	259-274	16
β-strand	281-284	4	1
α-helix	285-287	3
β-strand	293-299	7	1
β-strand	303-314	12	1
α-helix	317-319	3
α-helix	320-322	3
α-helix	334-340	7
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

Chain B: 20 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	150-157	8
α-helix	159-160	2
α-helix	161-184	24
β-strand	193-197	5	5
β-strand	211-219	9	5
β-strand	223-227	5	5
β-strand	234-239	6	5
α-helix	240-242	3
α-helix	249-251	3
β-strand	252-253	2	5
β-strand	256-257	2	5
α-helix	259-274	16
β-strand	281-284	4	5
α-helix	285-287	3
β-strand	293-299	7	5
β-strand	303-314	12	5
α-helix	317-319	3
α-helix	320-322	3
α-helix	334-340	7
β-strand	345-349	5	5
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	6
β-strand	474	1	6
α-helix	483-498	16
α-helix	502-505	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cyclic GMP-AMP synthase	A, B	protein	362	Mus musculus	Q8C6L5 (AlphaFold model)
DNA1	C, D	DNA	17
DNA2	E, F	DNA	17

Sequence of entity 1 (A, B), FASTA

>4O6A_1 Cyclic GMP-AMP synthase (chains A, B)
MPDKLKKVLDKLRLKRKDISEAAETVNKVVERLLRRMQKRESEFKGVEQLNTGSYYEHVK
ISAPNEFDVMFKLEVPRIELQEYYETGAFYLVKFKRIPRGNPLSHFLEGEVLSATKMLSK
FRKIIKEEVKEIKDIDVSVEKEKPGSPAVTLLIRNPEEISVDIILALESKGSWPISTKEG
LPIQGWLGTKVRTNLRREPFYLVPKNAKDGNSFQGETWRLSFSHTEKYILNNHGIEKTCC
ESSGAKCCRKECLKLMKYLLEQLKKEFQELDAFCSYHVKTAIFHMWTQDPQDSQWDPRNL
SSCFDKLLAFFLECLRTEKLDHYFIPKFNLFSQELIDRKSKEFLSKKIEYERNNGFPIFD
KL

Sequence of entity 2 (C, D), FASTA

>4O6A_2 DNA1 (chains C, D)
AAATTGCCGAAGACGAA

Sequence of entity 3 (E, F), FASTA

>4O6A_3 DNA2 (chains E, F)
TTTCGTCTTCGGCAATT

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	2

Primary citation

The Cytosolic DNA Sensor cGAS Forms an Oligomeric Complex with DNA and Undergoes Switch-like Conformational Changes in the Activation Loop. Zhang, X., Wu, J., Du, F. et al. Cell Rep (2014) 6:421-430. DOI 10.1016/j.celrep.2014.01.003 · PubMed

Other PDB entries of the same protein (UniProt Q8C6L5 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8SHK 1.71 Å, Structure of binary complex of mouse cGAS and bound ATP
8SHU 1.71 Å, Structure of mouse cGAS
8SHY 1.77 Å, Structure of binary complex of mouse cGAS QN and bound ATP
5XZG 1.83 Å, Mouse cGAS bound to the inhibitor RU521
4K98 1.94 Å, Structure of Ternary Complex of cGAS with dsDNA and Bound 5 -pppG(2 ,5 )pG
4K99 1.95 Å, Structure of Ternary Complex of cGAS with dsDNA and Bound 5 -pppdG(2 ,5 )pdG
4K8V 2.0 Å, Structure of cyclic GMP-AMP Synthase (cGAS)
7UTT 2.04 Å, Structure of Non-hydrolyzable ATP (ApCpp) binds to Cyclic GMP AMP synthase (cGAS)…
4K96 2.08 Å, Structure of Binary Complex of cGAS with Bound dsDNA
5XZB 2.13 Å, Mouse cGAS bound to the inhibitor RU365
7BUJ 2.13 Å, mcGAS bound with pppGpG
5XZE 2.18 Å, Mouse cGAS bound to the inhibitor RU332

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