1AB8: Adenylyl cyclase

Rat type II adenylyl cyclase C2 domain/forskolin complex. Determined by X-ray diffraction at 2.2 Å resolution. Released 15 May 1997.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Rattus norvegicus
Chains: 2
Atoms: 2,885
Mol. weight: 49.72 kDa
Ligands: FOK
Released: 15 May 1997

Explore 1AB8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1AB8 contains 14 α-helices and 13 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: 7 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	879-891	13	1
α-helix	895-898	4
α-helix	909-923	15
α-helix	924-927	4
α-helix	929-931	3
β-strand	934-940	7	1
β-strand	943-948	6	1
α-helix	967-987	21
β-strand	997-1010	14	1
β-strand	1016-1020	5	1
α-helix	1022-1032	11
β-strand	1039-1041	3	1
α-helix	1043-1052	10

Chain B: 7 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	879-891	13	2
α-helix	895-898	4
α-helix	909-923	15
α-helix	924-927	4
α-helix	929-931	3
β-strand	934-940	7	2
β-strand	943-948	6	2
α-helix	967-987	21
β-strand	997-1010	14	2
β-strand	1016-1020	5	2
α-helix	1022-1032	11
β-strand	1039-1041	3	2
α-helix	1043-1052	10
β-strand	1073	1	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Adenylyl cyclase	A, B	protein	220	Rattus norvegicus	P26769 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1AB8_1 ADENYLYL CYCLASE (chains A, B)
SLKNEELYHQSYDCVCVMFASIPDFKEFYTESDVNKEGLECLRLLNEIIADFDDLLSKPK
FSGVEKIKTIGSTYMAATGLSAIPSQEHAQEPERQYMHIGTMVEFAYALVGKLDAINKHS
FNDFKLRVGINHGPVIAGVIGAQKPQYDIWGNTVNVASRMDSTGVLDKIQVTEETSLILQ
TLGYTCTCRGIINVKGKGDLKTYFVNTEMSRSLSQSNLAS

Ligands and cofactors

ID	Name	Formula	Copies
FOK	Forskolin	C22 H34 O7	2

Primary citation

Structure of the adenylyl cyclase catalytic core. Zhang, G., Liu, Y., Ruoho, A.E. et al. Nature (1997) 386:247-253. DOI 10.1038/386247a0 · PubMed

Other PDB entries of the same protein (UniProt P26769 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1AZS 2.3 Å, Complex of gs-alpha with the catalytic domains of mammalian adenylyl cyclase
1CUL 2.4 Å, Complex of gs-alpha with the catalytic domains of mammalian adenylyl cyclase: complex…
1CS4 2.5 Å, Complex of gs-alpha with the catalytic domains of mammalian adenylyl cyclase: complex…
3C14 2.68 Å, Complex of GS-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex…
3C15 2.78 Å, Complex of GS-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex…
1CJT 2.8 Å, Complex of gs-alpha with the catalytic domains of mammalian adenylyl cyclase: complex…
1CJU 2.8 Å, Complex of gs-alpha with the catalytic domains of mammalian adenylyl cyclase: complex…
1TL7 2.8 Å, Complex Of Gs- With The Catalytic Domains Of Mammalian Adenylyl Cyclase: Complex With…
3C16 2.87 Å, Complex of GS-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex…
1U0H 2.9 Å, Structural basis for the inhibition of mammalian adenylyl cyclase by mant-GTP
2GVD 2.9 Å, Complex Of Gs- With The Catalytic Domains Of Mammalian Adenylyl Cyclase: Complex With…
1CJK 3.0 Å, Complex of gs-alpha with the catalytic domains of mammalian adenylyl cyclase: complex…

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