1cs4

COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE: COMPLEX WITH 2'-DEOXY-ADENOSINE 3'-MONOPHOSPHATE, PYROPHOSPHATE AND MG

Method: X-RAY DIFFRACTION

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1. Protein Identity and Related Structures Protein Identity & Related Structures

TYPE V ADENYLATE CYCLASE

Canis lupus familiaris

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 3	TYPE II ADENYLATE CYCLASE × 1 （P26769） GUANINE NUCLEOTIDE-BINDING PROTEIN G(S) × 1 （P04896） MAGNESIUM ION × 2 FORSKOLIN × 1 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 PYROPHOSPHATE 2- × 1 ;2'-DEOXY-ADENOSINE 3'-MONOPHOSPHATE ; × 1 CHLORIDE ION × 1 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE × 1 water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ADCY5_CANFA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 8–225； UniProt 363–580

TYPE II ADENYLATE CYCLASE

Rattus norvegicus

UniProt P26769

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 3	TYPE V ADENYLATE CYCLASE × 1 （P30803） GUANINE NUCLEOTIDE-BINDING PROTEIN G(S) × 1 （P04896） MAGNESIUM ION × 2 FORSKOLIN × 1 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 PYROPHOSPHATE 2- × 1 ;2'-DEOXY-ADENOSINE 3'-MONOPHOSPHATE ; × 1 CHLORIDE ION × 1 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE × 1 water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ADCY2_RAT
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–212； UniProt 870–1081

GUANINE NUCLEOTIDE-BINDING PROTEIN G(S)

Bos taurus

UniProt P04896

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 3	TYPE V ADENYLATE CYCLASE × 1 （P30803） TYPE II ADENYLATE CYCLASE × 1 （P26769） MAGNESIUM ION × 2 FORSKOLIN × 1 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 PYROPHOSPHATE 2- × 1 ;2'-DEOXY-ADENOSINE 3'-MONOPHOSPHATE ; × 1 CHLORIDE ION × 1 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE × 1 water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	GNAS_BOVIN
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain C； PDBConstruct 1–394； UniProt 1–394

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1cs4
Deposition date deposition_date	1999-08-16
Structure title title	COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE: COMPLEX WITH 2'-DEOXY-ADENOSINE 3'-MONOPHOSPHATE, PYROPHOSPHATE AND MG
Keywords keywords	;COMPLEX (LYASE-HYDROLASE), HYDROLASE, SIGNAL TRANSDUCING PROTEIN, CYCLASE, EFFECTOR ENZYME, LYASE-HYDROLASE COMPLEX, LYASE-LYASE-SIGNALING PROTEIN COMPLEX ;; LYASE/LYASE/SIGNALING PROTEIN
Experimental Method method	X-RAY DIFFRACTION

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

1cs4__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1cs4__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1cs4__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	32.05 Å
Rg (electron density)	31.40 Å
Total Rg	31.97 Å
Atom count	5766
Residues	708
Excluded volume	102490 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1cs4__assembly_1__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (11)

Entity 1 Entity 1 polymer

Description description	TYPE V ADENYLATE CYCLASE
Molecular weight formula_weight	25526.5 kDa
EC 编号 ec_number	4.6.1.1
Mutation mutation	V476M
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	5843

MHHHHHHAMEMKADINAKQEDMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGMDMIEAISLVREMTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLSYLNGDYEVEPGCGGERNAYLKEHSIETFLILRCTQKRKEEKAMIAK

Source Source

Source organism organism	Canis lupus familiaris
Common name common_name	dog
NCBI taxonomy ID ncbi_taxonomy_id	9615
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	TYPE II ADENYLATE CYCLASE
Molecular weight formula_weight	23717.0 kDa
EC 编号 ec_number	4.6.1.1
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

RSLKNEELYHQSYDCVCVMFASIPDFKEFYTESDVNKEGLECLRLLNEIIADFDDLLSKPKFSGVEKIKTIGSTYMAATGLSAIPSQEHAQEPERQYMHIGTMVEFAYALVGKLDAINKHSFNDFKLRVGINHGPVIAGVIGAQKPQYDIWGNTVNVASRMDSTGVLDKIQVTEETSLILQTLGYTCTCRGIINVKGKGDLKTYFVNTEMSR

Source Source

Source organism organism	Rattus norvegicus
Common name common_name	Norway rat
NCBI taxonomy ID ncbi_taxonomy_id	10116
Host organism host_organism	Escherichia coli

Entity 3 Entity 3 polymer

Description description	GUANINE NUCLEOTIDE-BINDING PROTEIN G(S)
Molecular weight formula_weight	45769.5 kDa
Mutation mutation	TRYPSINIZED, SHORT FORM
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C

MGCLGNSKTEDQRNEEKAQREANKKIEKQLQKDKQVYRATHRLLLLGAGESGKSTIVKQMRILHVNGFNGEGGEEDPQAARSNSDGEKATKVQDIKNNLKEAIETIVAAMSNLVPPVELANPENQFRVDYILSVMNVPDFDFPPEFYEHAKALWEDEGVRACYERSNEYQLIDCAQYFLDKIDVIKQDDYVPSDQDLLRCRVLTSGIFETKFQVDKVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASSSYNMVIREDNQTNRLQEALNLFKSIWNNRWLRTISVILFLNKQDLLAEKVLAGKSKIEDYFPEFARYTTPEDATPEPGEDPRVTRAKYFIRDEFLRISTASGDGRHYCYPHFTCAVDTENIRRVFNDCRDIIQRMHLRQYELL

Source Source

Source organism organism	Bos taurus
Common name common_name	cattle
NCBI taxonomy ID ncbi_taxonomy_id	9913
Host organism host_organism	Escherichia coli

Entity 4 Entity 4 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 5 Entity 5 non-polymer

Description description	FORSKOLIN
Molecular weight formula_weight	410.5 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 6 Entity 6 non-polymer

Description description	2-(N-MORPHOLINO)-ETHANESULFONIC ACID
Molecular weight formula_weight	195.2 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 7 Entity 7 non-polymer

Description description	PYROPHOSPHATE 2-
Molecular weight formula_weight	176.0 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 8 Entity 8 non-polymer

Description description	;2'-DEOXY-ADENOSINE 3'-MONOPHOSPHATE ;
Molecular weight formula_weight	331.2 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 9 Entity 9 non-polymer

Description description	CHLORIDE ION
Molecular weight formula_weight	35.5 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 10 Entity 10 non-polymer

Description description	5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE
Molecular weight formula_weight	539.2 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 11 Entity 11 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	77

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6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1cs4a_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.58 — Ferredoxin-like
Superfamily Superfamily superfamily	d.58.29 — Nucleotide cyclase
Family Family family	d.58.29.1 — Adenylyl and guanylyl cyclase catalytic domain

Domain ID domain_id	d1cs4b_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.58 — Ferredoxin-like
Superfamily Superfamily superfamily	d.58.29 — Nucleotide cyclase
Family Family family	d.58.29.1 — Adenylyl and guanylyl cyclase catalytic domain

Domain ID domain_id	d1cs4c1
Class class	a — All alpha proteins
Fold Fold fold	a.66 — Transducin (alpha subunit), insertion domain
Superfamily Superfamily superfamily	a.66.1 — Transducin (alpha subunit), insertion domain
Family Family family	a.66.1.1 — Transducin (alpha subunit), insertion domain

Domain ID domain_id	d1cs4c2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamily	c.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family family	c.37.1.8 — G proteins

CATH v4.4 (4 domains)

Domain ID domain_id	1cs4A00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	1230 — Nucleotide cyclase, GGDEF domain

Domain ID domain_id	1cs4B00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	1230 — Nucleotide cyclase, GGDEF domain

Domain ID domain_id	1cs4C01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	1cs4C02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	400 — GI Alpha 1, domain 2-like
Homologous superfamily homologous superfamily	10 — GI Alpha 1, domain 2-like

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Unit-cell length a length_a	118.500 Å
Unit-cell length b length_b	134.500 Å
Unit-cell length c length_c	71.300 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 21 21 2
Space-group number int_tables_number	18
Crystal system crystal_system	—

Resolution resolution	2.500 Å
Low-resolution limit resolution_low	15.000 Å
R factor r_factor	0.2210
R_work r_work	0.2160
R_free r_free	0.2640

COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE: COMPLEX WITH 2'-DEOXY-ADENOSINE 3'-MONOPHOSPHATE, PYROPHOSPHATE AND MG

1. Protein Identity and Related Structures Protein Identity & Related Structures

TYPE V ADENYLATE CYCLASE

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

TYPE II ADENYLATE CYCLASE

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

GUANINE NUCLEOTIDE-BINDING PROTEIN G(S)

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1cs4__assembly_1__model_1

1cs4__assembly_1__model_1 | I(q)

1cs4__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (11)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 polymer

Polymer Polymer

Source Source

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 non-polymer

Entity 8 Entity 8 non-polymer

Entity 9 Entity 9 non-polymer

Entity 10 Entity 10 non-polymer

Entity 11 Entity 11 water

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (2)