3MAA: Adenylate cyclase type 5

Complex of GS-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Adenosine 5-O-(l-Thiophosphate) and Low Ca Concentration. Determined by X-ray diffraction at 3.0 Å resolution. Released 7 Apr 2010.

Method: X-ray diffraction
Resolution: 3.0 Å
Organisms: Canis lupus familiaris, Rattus norvegicus, Bos taurus
Chains: 3
Atoms: 5,744
Mol. weight: 96.73 kDa
Ligands: FKP, CA, TAT, MG
Released: 7 Apr 2010

Explore 3MAA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3MAA contains 32 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: 8 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	380-381	2
β-strand	384	1	1
β-strand	387-398	12	2
α-helix	400-406	7
α-helix	409-430	22
β-strand	433-438	6	2
β-strand	441-446	6	2
α-helix	455-475	21
β-strand	482-492	11	2
β-strand	494-495	2	1
β-strand	505-506	2	1
α-helix	509-519	11
β-strand	527-528	2	2
α-helix	530-534	5
β-strand	542-544	3	2
α-helix	547-549	3
α-helix	552-555	4
β-strand	562-564	3	2

Chain B: 6 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	881	1	3
β-strand	885-891	7	4
α-helix	895-898	4
β-strand	902	1	5
β-strand	906	1	5
α-helix	909-927	19
α-helix	929-931	3
β-strand	935-940	6	4
β-strand	943-948	6	4
α-helix	967-990	24
β-strand	997-1003	7	4
β-strand	1006-1010	5	3
β-strand	1016-1020	5	3
α-helix	1022-1032	11
β-strand	1038-1042	5	4
α-helix	1043-1050	8
β-strand	1056-1064	9	4
β-strand	1068-1075	8	4

Chain C: 18 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	40-47	8	6
α-helix	53-64	12
α-helix	89-111	23
α-helix	122-124	3
α-helix	125-132	8
α-helix	145-155	11
α-helix	157-163	7
α-helix	166-168	3
α-helix	175-179	5
α-helix	182-186	5
α-helix	194-199	6
β-strand	207-213	7	6
β-strand	218-224	7	6
α-helix	228-233	6
α-helix	235-237	3
β-strand	243-249	7	6
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	308-311	4
α-helix	313-316	4
α-helix	332-350	19
β-strand	359-364	6	6
α-helix	369-383	15

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Adenylate cyclase type 5	A	protein	225	Canis lupus familiaris	P30803 (AlphaFold model)
Adenylate cyclase type 2	B	protein	212	Rattus norvegicus	P26769 (AlphaFold model)
Guanine nucleotide-binding protein G(s) subunit alpha isoforms short	C	protein	394	Bos taurus	P04896 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3MAA_1 Adenylate cyclase type 5 (chains A)
MHHHHHHAMEMKADINAKQEDMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMT
LNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGMDMIEAISLVRE
MTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLSY
LNGDYEVEPGCGGERNAYLKEHSIETFLILRCTQKRKEEKAMIAK

Sequence of entity 2 (B), FASTA

>3MAA_2 Adenylate cyclase type 2 (chains B)
RSLKNEELYHQSYDCVCVMFASIPDFKEFYTESDVNKEGLECLRLLNEIIADFDDLLSKP
KFSGVEKIKTIGSTYMAATGLSAIPSQEHAQEPERQYMHIGTMVEFAYALVGKLDAINKH
SFNDFKLRVGINHGPVIAGVIGAQKPQYDIWGNTVNVASRMDSTGVLDKIQVTEETSLIL
QTLGYTCTCRGIINVKGKGDLKTYFVNTEMSR

Sequence of entity 3 (C), FASTA

>3MAA_3 Guanine nucleotide-binding protein G(s) subunit alpha isoforms short (chains C)
MGCLGNSKTEDQRNEEKAQREANKKIEKQLQKDKQVYRATHRLLLLGAGESGKSTIVKQM
RILHVNGFNGEGGEEDPQAARSNSDGEKATKVQDIKNNLKEAIETIVAAMSNLVPPVELA
NPENQFRVDYILSVMNVPDFDFPPEFYEHAKALWEDEGVRACYERSNEYQLIDCAQYFLD
KIDVIKQDDYVPSDQDLLRCRVLTSGIFETKFQVDKVNFHMFDVGGQRDERRKWIQCFND
VTAIIFVVASSSYNMVIREDNQTNRLQEALNLFKSIWNNRWLRTISVILFLNKQDLLAEK
VLAGKSKIEDYFPEFARYTTPEDATPEPGEDPRVTRAKYFIRDEFLRISTASGDGRHYCY
PHFTCAVDTENIRRVFNDCRDIIQRMHLRQYELL

Ligands and cofactors

ID	Name	Formula	Copies
FKP	Methylpiperazinoforskolin	C30 H50 N2 O7	1
CA	Calcium ion	Ca	1
TAT	Adenosine-5'-rp-alpha-thio-triphosphate	C10 H16 N5 O12 P3 S	1
MG	Magnesium ion	Mg	1
GSP	5'-guanosine-diphosphate-monothiophosphate	C10 H16 N5 O13 P3 S	1

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

Primary citation

Structural basis for inhibition of mammalian adenylyl cyclase by calcium. Mou, T.C., Masada, N., Cooper, D.M. et al. Biochemistry (2009) 48:3387-3397. DOI 10.1021/bi802122k · 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…
1CJK 3.0 Å, Complex of gs-alpha with the catalytic domains of mammalian adenylyl cyclase: complex…

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