4K9A: Cyclic GMP-AMP synthase

Structure of Ternary Complex of cGAS with dsDNA and Bound 5 -pG(2 ,5 )pA. Determined by X-ray diffraction at 2.26 Å resolution. Released 15 May 2013.

Method: X-ray diffraction
Resolution: 2.26 Å
Organism: Mus musculus
Chains: 3
Atoms: 3,767
Mol. weight: 53.8 kDa
Ligands: AMP, 5GP, PO4, ZN
Released: 15 May 2013

Explore 4K9A in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4K9A contains 19 α-helices and 15 β-strands across 1 chain. 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	150-157	8
α-helix	159-160	2
α-helix	161-183	23
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	247-251	5
β-strand	252-253	2	1
β-strand	256-257	2	1
α-helix	259-275	17
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	345-348	4	1
α-helix	350-352	3
β-strand	353-354	2	2
β-strand	357-358	2	2
β-strand	363-366	4	1
α-helix	368-376	9
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	3
β-strand	474	1	3
α-helix	483-498	16
α-helix	502-505	4

Molecules and chains

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

Sequence of entity 1 (A), FASTA

>4K9A_1 Cyclic GMP-AMP synthase (chains A)
SPDKLKKVLDKLRLKRKDISEAAETVNKVVERLLRRMQKRESEFKGVEQLNTGSYYEHVK
ISAPNEFDVMFKLEVPRIELQEYYETGAFYLVKFKRIPRGNPLSHFLEGEVLSATKMLSK
FRKIIKEEVKEIKDIDVSVEKEKPGSPAVTLLIRNPEEISVDIILALESKGSWPISTKEG
LPIQGWLGTKVRTNLRREPFYLVPKNAKDGNSFQGETWRLSFSHTEKYILNNHGIEKTCC
ESSGAKCCRKECLKLMKYLLEQLKKEFQELDAFCSYHVKTAIFHMWTQDPQDSQWDPRNL
SSCFDKLLAFFLECLRTEKLDHYFIPKFNLFSQELIDRKSKEFLSKKIEYERNNGFPIFD
KL

Sequence of entity 2 (D), FASTA

>4K9A_2 DNA-F (chains D)
AAATTGCCGAAGACGAA

Sequence of entity 3 (E), FASTA

>4K9A_3 DNA-R (chains E)
TTTCGTCTTCGGCAATT

Ligands and cofactors

ID	Name	Formula	Copies
AMP	Adenosine monophosphate	C10 H14 N5 O7 P	1
5GP	Guanosine-5'-monophosphate	C10 H14 N5 O8 P	1
PO4	Phosphate ion	O4 P	1
ZN	Zinc ion	Zn	1

Primary citation

Cyclic [G(2',5')pA(3',5')p] is the metazoan second messenger produced by DNA-activated cyclic GMP-AMP synthase. Gao, P., Ascano, M., Wu, Y. et al. Cell (2013) 153:1094-1107. DOI 10.1016/j.cell.2013.04.046 · 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
4O6A 1.86 Å, Mouse cyclic GMP-AMP synthase (cGAS) in complex with DNA
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

Browse structure collections

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