1U0H: Adenylate cyclase, type V

Structural basis for the inhibition of mammalian adenylyl cyclase by mant-GTP. Determined by X-ray diffraction at 2.9 Å resolution. Released 14 Dec 2004.

Method: X-ray diffraction
Resolution: 2.9 Å
Organisms: Canis lupus familiaris, Rattus norvegicus, Bos taurus
Chains: 3
Atoms: 5,769
Mol. weight: 96.73 kDa
Ligands: GSP, ONM, FOK, MG
Released: 14 Dec 2004

Explore 1U0H in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1U0H contains 31 α-helices and 30 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: 7 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	380-382	3
β-strand	383-396	14	1
β-strand	397-398	2	2
α-helix	409-429	21
β-strand	434-438	5	1
β-strand	441-446	6	1
α-helix	455-476	22
β-strand	482-483	2	2
β-strand	485-496	12	1
β-strand	505-506	2	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, 11 β-strands

Element	Residues	Length	Sheet
β-strand	882-891	10	3
α-helix	895-898	4
α-helix	903-905	3
α-helix	909-923	15
α-helix	929-931	3
β-strand	934-940	7	3
β-strand	943-948	6	3
α-helix	968-990	23
β-strand	997-1005	9	3
β-strand	1006	1	4
β-strand	1009-1010	2	5
β-strand	1016-1017	2	5
β-strand	1020	1	4
α-helix	1022-1032	11
β-strand	1039-1042	4	3
α-helix	1043-1050	8
β-strand	1056-1064	9	3
β-strand	1068-1075	8	3

Chain C: 17 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	43-47	5	6
α-helix	53-64	12
α-helix	88-112	25
α-helix	125-133	9
α-helix	144-155	12
α-helix	157-163	7
α-helix	166-168	3
α-helix	175-179	5
α-helix	182-185	4
α-helix	195-199	5
β-strand	208-213	6	6
β-strand	218-223	6	6
α-helix	231-237	7
β-strand	243-249	7	6
α-helix	252-254	3
β-strand	256	1	7
β-strand	264	1	7
α-helix	265-277	13
β-strand	287-292	6	6
α-helix	294-303	10
α-helix	308-310	3
α-helix	313-315	3
α-helix	332-351	20
β-strand	359	1	6
β-strand	363	1	6
α-helix	369-385	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Adenylate cyclase, type V	A	protein	225	Canis lupus familiaris	P30803 (AlphaFold model)
Adenylate cyclase, type II	B	protein	212	Rattus norvegicus	P26769 (AlphaFold model)
Guanine nucleotide-binding protein G(s), alpha subunit	C	protein	394	Bos taurus	P04896 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1U0H_1 Adenylate cyclase, type V (chains A)
MHHHHHHAMEMKADINAKQEDMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMT
LNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGMDMIEAISLVRE
MTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLSY
LNGDYEVEPGCGGERNAYLKEHSIETFLILRCTQKRKEEKAMIAK

Sequence of entity 2 (B), FASTA

>1U0H_2 Adenylate cyclase, type II (chains B)
RSLKNEELYHQSYDCVCVMFASIPDFKEFYTESDVNKEGLECLRLLNEIIADFDDLLSKP
KFSGVEKIKTIGSTYMAATGLSAIPSQEHAQEPERQYMHIGTMVEFAYALVGKLDAINKH
SFNDFKLRVGINHGPVIAGVIGAQKPQYDIWGNTVNVASRMDSTGVLDKIQVTEETSLIL
QTLGYTCTCRGIINVKGKGDLKTYFVNTEMSR

Sequence of entity 3 (C), FASTA

>1U0H_3 Guanine nucleotide-binding protein G(s), alpha subunit (chains C)
MGCLGNSKTEDQRNEEKAQREANKKIEKQLQKDKQVYRATHRLLLLGAGESGKSTIVKQM
RILHVNGFNGEGGEEDPQAARSNSDGEKATKVQDIKNNLKEAIETIVAAMSNLVPPVELA
NPENQFRVDYILSVMNVPDFDFPPEFYEHAKALWEDEGVRACYERSNEYQLIDCAQYFLD
KIDVIKQDDYVPSDQDLLRCRVLTSGIFETKFQVDKVNFHMFDVGGQRDERRKWIQCFND
VTAIIFVVASSSYNMVIREDNQTNRLQEALNLFKSIWNNRWLRTISVILFLNKQDLLAEK
VLAGKSKIEDYFPEFARYTTPEDATPEPGEDPRVTRAKYFIRDEFLRISTASGDGRHYCY
PHFTCAVDTENIRRVFNDCRDIIQRMHLRQYELL

Ligands and cofactors

ID	Name	Formula	Copies
GSP	5'-guanosine-diphosphate-monothiophosphate	C10 H16 N5 O13 P3 S	1
ONM	3'-O-(N-methylanthraniloyl)-guanosine-5'-triphosphate	C18 H23 N6 O15 P3	1
FOK	Forskolin	C22 H34 O7	1
MG	Magnesium ion	Mg	3

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

Primary citation

Structural basis for the inhibition of mammalian membrane adenylyl cyclase by 2 '(3')-O-(N-Methylanthraniloyl)-guanosine 5 '-triphosphate. Mou, T.C., Gille, A., Fancy, D.A. et al. J Biol Chem (2005) 280:7253-7261. DOI 10.1074/jbc.M409076200 · 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…
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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