1CJK: Adenylate cyclase, type V

Complex of gs-alpha with the catalytic domains of mammalian adenylyl cyclase: complex with adenosine 5'-(alpha thio)-triphosphate (RP), MG, and MN. Determined by X-ray diffraction at 3.0 Å resolution. Released 31 Aug 1999.

Method: X-ray diffraction
Resolution: 3.0 Å
Organisms: Canis lupus familiaris, Rattus norvegicus, Bos taurus
Chains: 3
Atoms: 5,799
Mol. weight: 96.68 kDa
Ligands: MG, MN, FOK, TAT
Released: 31 Aug 1999

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

Secondary structure: helices and β-sheets

1CJK contains 33 α-helices and 28 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, 8 β-strands

Element	Residues	Length	Sheet
α-helix	380-382	3
β-strand	383-397	15	1
α-helix	400-403	4
α-helix	409-429	21
β-strand	432-438	7	1
β-strand	441-446	6	1
α-helix	455-477	23
β-strand	483-496	14	1
β-strand	505-507	3	1
α-helix	509-519	11
β-strand	526-529	4	1
α-helix	530-533	4
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, 12 β-strands

Element	Residues	Length	Sheet
β-strand	880-881	2	2
β-strand	885-890	6	3
β-strand	891	1	4
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	3
β-strand	943-948	6	3
α-helix	967-990	24
β-strand	997	1	4
β-strand	998-1003	6	3
β-strand	1006-1008	3	2
β-strand	1018-1020	3	2
α-helix	1022-1032	11
β-strand	1039-1042	4	3
α-helix	1043-1051	9
β-strand	1056-1064	9	3
β-strand	1068-1075	8	3

Chain C: 18 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	40-46	7	5
α-helix	53-64	12
α-helix	88-109	22
α-helix	116-119	4
α-helix	124-133	10
α-helix	144-154	11
α-helix	157-164	8
α-helix	166-168	3
α-helix	175-179	5
α-helix	182-186	5
α-helix	194-199	6
β-strand	208-213	6	5
β-strand	218-223	6	5
α-helix	228-237	10
β-strand	243-249	7	5
β-strand	256	1	6
β-strand	264	1	6
α-helix	265-277	13
β-strand	287-292	6	5
α-helix	294-303	10
α-helix	308-310	3
α-helix	313-317	5
α-helix	326-327	2
α-helix	332-350	19
β-strand	359-363	5	5
α-helix	369-385	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Adenylate cyclase, type V	A	protein	217	Canis lupus familiaris	P30803 (AlphaFold model)
Adenylate cyclase, type II	B	protein	212	Rattus norvegicus	P26769 (AlphaFold model)
Guanine nucleotide-binding protein g(s)	C	protein	402	Bos taurus	P04896 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1CJK_1 ADENYLATE CYCLASE, TYPE V (chains A)
MEMKADINAKQEDMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARF
DKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGMDMIEAISLVREMTGVNVNM
RVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLSYLNGDYEVE
PGCGGERNAYLKEHSIETFLILRCTQKRKEEKAMIAK

Sequence of entity 2 (B), FASTA

>1CJK_2 ADENYLATE CYCLASE, TYPE II (chains B)
RSLKNEELYHQSYDCVCVMFASIPDFKEFYTESDVNKEGLECLRLLNEIIADFDDLLSKP
KFSGVEKIKTIGSTYMAATGLSAIPSQEHAQEPERQYMHIGTMVEFAYALVGKLDAINKH
SFNDFKLRVGINHGPVIAGVIGAQKPQYDIWGNTVNVASRMDSTGVLDKIQVTEETSLIL
QTLGYTCTCRGIINVKGKGDLKTYFVNTEMSR

Sequence of entity 3 (C), FASTA

>1CJK_3 GUANINE NUCLEOTIDE-BINDING PROTEIN G(S) (chains C)
MGCLGNSKTEDQRNEEKAQREANKKIEKQLQKDKQVYRATHRLLLLGAGESGKSTIVKQM
RILHVNGFNGGEGGEEDPNAKSNSDGEKATKVQDIKNNLKEAIETIVAAMSNLVPPVELA
NPENQFRVDYILSVMNVPDFDFPPEFYEHAKALWEDEGVRACYERSNEYQLIDCAQYFLD
KIDVIKQDDYVPSDQDLLRCRVLTSGIFETKFQVDKVNFHMFDVGGQRDERRKWIQCFND
VTAIIFVVASSSYNMVIREDNQTNRLQEALNLFKSIWNNRWLRTISVILFLNKQDLLAEK
VLAGKSKIEDYFPEFARYTTPEDATPEPGEDPRVTRAKYFIRDEFLRISTASGDGRHYCY
PHFTCAVDTENIRRVFNDCRDIIQRMHLRQYELLGGHHHHHH

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	2
MN	Manganese (II) ion	Mn	1
FOK	Forskolin	C22 H34 O7	1
TAT	Adenosine-5'-rp-alpha-thio-triphosphate	C10 H16 N5 O12 P3 S	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

Two-metal-Ion catalysis in adenylyl cyclase. Tesmer, J.J., Sunahara, R.K., Johnson, R.A. et al. Science (1999) 285:756-760. DOI 10.1126/science.285.5428.756 · 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
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…
1CJV 3.0 Å, Complex of gs-alpha with the catalytic domains of mammalian adenylyl cyclase: complex…

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