1CUL: Type V adenylyl cyclase

Complex of gs-alpha with the catalytic domains of mammalian adenylyl cyclase: complex with 2',5'-dideoxy-adenosine 3'-triphosphate and MG. Determined by X-ray diffraction at 2.4 Å resolution. Released 10 Jan 2001.

Method: X-ray diffraction
Resolution: 2.4 Å
Organisms: Canis lupus familiaris, Rattus norvegicus, Bos taurus
Chains: 3
Atoms: 5,847
Mol. weight: 94.12 kDa
Ligands: MG, FOK, 3PO, 103
Released: 10 Jan 2001

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

Secondary structure: helices and β-sheets

1CUL contains 34 α-helices and 25 β-strands across 3 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: 8 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	380-382	3
β-strand	384-397	14	1
α-helix	400-406	7
α-helix	409-429	21
β-strand	432-438	7	1
β-strand	441-446	6	1
α-helix	455-477	23
β-strand	483-495	13	1
β-strand	505-507	3	1
α-helix	509-519	11
β-strand	523	1	1
β-strand	526-529	4	1
α-helix	530-535	6
β-strand	542-544	3	1
α-helix	547-549	3
α-helix	552-556	5
β-strand	561-564	4	1

Chain B: 7 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	880-891	12	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	967-989	23
β-strand	997-1008	12	2
β-strand	1018-1020	3	2
α-helix	1022-1032	11
β-strand	1039-1042	4	2
α-helix	1043-1050	8
β-strand	1056-1064	9	2
β-strand	1068-1075	8	2

Chain C: 19 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	40-46	7	3
α-helix	53-64	12
α-helix	91-110	20
α-helix	116-119	4
α-helix	124-134	11
α-helix	144-155	12
α-helix	157-164	8
α-helix	166-168	3
α-helix	175-179	5
α-helix	182-185	4
α-helix	194-199	6
β-strand	207-214	8	3
β-strand	217-224	8	3
α-helix	228-237	10
β-strand	243-249	7	3
α-helix	250-254	5
β-strand	256	1	4
β-strand	264	1	4
α-helix	265-277	13
β-strand	287-292	6	3
α-helix	294-303	10
α-helix	308-310	3
α-helix	313-316	4
α-helix	326-327	2
α-helix	332-350	19
β-strand	359-363	5	3
α-helix	369-385	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Type V adenylyl cyclase	A	protein	217	Canis lupus familiaris	P30803 (AlphaFold model)
Type II adenylyl cyclase	B	protein	208	Rattus norvegicus	P26769 (AlphaFold model)
Guanine nucleotide-binding protein g(s)	C	protein	380	Bos taurus	P04896 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1CUL_1 TYPE V ADENYLYL CYCLASE (chains A)
MEMKADINAKQEDMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARF
DKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGMDMIEAISLVREMTGVNVNM
RVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLSYLNGDYEVE
PGCGGERNAYLKEHSIETFLILRCTQKRKEEKAMIAK

Sequence of entity 2 (B), FASTA

>1CUL_2 TYPE II ADENYLYL CYCLASE (chains B)
NEELYHQSYDCVCVMFASIPDFKEFYTESDVNKEGLECLRLLNEIIADFDDLLSKPKFSG
VEKIKTIGSTYMAATGLSAIPSQEHAQEPERQYMHIGTMVEFAYALVGKLDAINKHSFND
FKLRVGINHGPVIAGVIGAQKPQYDIWGNTVNVASRMDSTGVLDKIQVTEETSLILQTLG
YTCTCRGIINVKGKGDLKTYFVNTEMSR

Sequence of entity 3 (C), FASTA

>1CUL_3 GUANINE NUCLEOTIDE-BINDING PROTEIN G(S) (chains C)
MGCLGNSKTEDQRNEEKAQREANKKIEKQLQKDKQVYRATHRLLLLGAGESGKSTIVKQM
RILHVNGFNGDGEKATKVQDIKNNLKEAIETIVAAMSNLVPPVELANPENQFRVDYILSV
MNVPDFDFPPEFYEHAKALWEDEGVRACYERSNEYQLIDCAQYFLDKIDVIKQDDYVPSD
QDLLRCRVLTSGIFETKFQVDKVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASSSYN
MVIREDNQTNRLQEALNLFKSIWNNRWLRTISVILFLNKQDLLAEKVLAGKSKIEDYFPE
FARYTTPEDATPEPGEDPRVTRAKYFIRDEFLRISTASGDGRHYCYPHFTCAVDTENIRR
VFNDCRDIIQRMHLRQYELL

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	3
FOK	Forskolin	C22 H34 O7	1
3PO	Triphosphate	H5 O10 P3	1
103	2',5'-dideoxy-adenosine 3'-monophosphate	C10 H14 N5 O5 P	1
GSP	5'-guanosine-diphosphate-monothiophosphate	C10 H16 N5 O13 P3 S	1

Water and common crystallization additives (MES, CL) are not listed.

Primary citation

Molecular basis for P-site inhibition of adenylyl cyclase. Tesmer, J.J., Dessauer, C.W., Sunahara, R.K. et al. Biochemistry (2000) 39:14464-14471. DOI 10.1021/bi0015562 · PubMed

Other PDB entries of the same protein (UniProt P30803 (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
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…
1CJV 3.0 Å, Complex of gs-alpha with the catalytic domains of mammalian adenylyl cyclase: complex…

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