1azs

COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE

Method: X-RAY DIFFRACTION Dmax: 102.0 Å Quality: GOOD

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

VC1

Canis lupus familiaris

UniProt P30803

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 442–656 Fragment:C1A DOMAIN OF ADENYLYL CYCLASE Mutation:V476M, N-TERMINAL HEXAHISTIDINE TAG IIC2 × 2 (P26769) GS-ALPHA × 2 (P04896) FKP METHYLPIPERAZINOFORSKOLIN × 2 MG MAGNESIUM ION × 2 GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.6;CRYSTALLIZED IN HANGING DROPS CONTAINING PROTEIN MIXED 1:1 WITH WELL SOLUTION OF 7.2-7.5% PEG 8000, 500MM NACL AND 100 MM (PH 5.4-5.6), vapor diffusion - hanging drop Resolution 2.30 Å R-free 0.282

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

15 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ADCY5_CANFA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–220; UniProt 442–656

IIC2

Rattus norvegicus

UniProt P26769

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 870–1081 Fragment:C2A DOMAIN OF ADENYLYL CYCLASE VC1 × 2 (P30803) GS-ALPHA × 2 (P04896) FKP METHYLPIPERAZINOFORSKOLIN × 2 MG MAGNESIUM ION × 2 GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.6;CRYSTALLIZED IN HANGING DROPS CONTAINING PROTEIN MIXED 1:1 WITH WELL SOLUTION OF 7.2-7.5% PEG 8000, 500MM NACL AND 100 MM (PH 5.4-5.6), vapor diffusion - hanging drop Resolution 2.30 Å R-free 0.282

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

16 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

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

GS-ALPHA

Bos taurus

UniProt P04896

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain C; UniProt 1–394 Mutation:C-TERMINAL HEXAHISTIDINE TAG, NOT PALMITOYLATED AT AMINO TERMINUS VC1 × 2 (P30803) IIC2 × 2 (P26769) FKP METHYLPIPERAZINOFORSKOLIN × 2 MG MAGNESIUM ION × 2 GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.6;CRYSTALLIZED IN HANGING DROPS CONTAINING PROTEIN MIXED 1:1 WITH WELL SOLUTION OF 7.2-7.5% PEG 8000, 500MM NACL AND 100 MM (PH 5.4-5.6), vapor diffusion - hanging drop Resolution 2.30 Å R-free 0.282

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

41 other PDB entries and 42 assemblies. Open the comparison page and filter oligomeric states

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.

SAXS scattering curve SAXS Profile

SAXS profile for 1azs

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1azs
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1azs
Deposition date deposition_date1997-11-20
Structure title titleCOMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE
Keywords keywordsCOMPLEX (LYASE-HYDROLASE), HYDROLASE, SIGNAL TRANSDUCING PROTEIN, CYCLASE, EFFECTOR ENZYME, COMPLEX (LYASE-HYDROLASE) complex; COMPLEX (LYASE/HYDROLASE)
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier32.08
Radius of gyration Rg (electron density) rg_electron31.38
Forward intensity I(0) i0110368000.00
Molecular weight molecular_weight82826.0 kDa
Excluded volume excluded_volume103400 ų
Envelope volume envelope_volume132670 ų
Hydration-shell volume shell_volume35307 ų
Envelope diameter envelope_diameter99.8
Shell Rg shell_rg38.20
Envelope Rg envelope_rg31.16
Shape Rg shape_rg31.38
Total Rg total_rg31.98
Total atoms total_atoms5812
Residues n_residues718
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax102.0
Rg (real space) rg_real32.08
Rg uncertainty (real space) rg_real_error0.76
I(0) (real space) i0_real1.1040e+08
I(0) uncertainty (real space) i0_real_error1.7760e+06
Rg (reciprocal space) rg_reciprocal32.08
I(0) (reciprocal space) i0_reciprocal110400000.0000
Solution quality estimate total_estimate0.8309
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary31.2
Skewness Skewness skewness0.255
Kurtosis Kurtosis kurtosis-0.678
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha22940000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.940; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.976; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1azsa_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.58 — Ferredoxin-like
Superfamily Superfamily superfamilyd.58.29 — Nucleotide cyclase
Family Family familyd.58.29.1 — Adenylyl and guanylyl cyclase catalytic domain
Domain ID domain_idd1azsb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.58 — Ferredoxin-like
Superfamily Superfamily superfamilyd.58.29 — Nucleotide cyclase
Family Family familyd.58.29.1 — Adenylyl and guanylyl cyclase catalytic domain
Domain ID domain_idd1azsc1
Class classa — All alpha proteins
Fold Fold folda.66 — Transducin (alpha subunit), insertion domain
Superfamily Superfamily superfamilya.66.1 — Transducin (alpha subunit), insertion domain
Family Family familya.66.1.1 — Transducin (alpha subunit), insertion domain
Domain ID domain_idd1azsc2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.8 — G proteins

CATH v4.4 (4 domains)

Domain ID domain_id1azsA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily1230 — Nucleotide cyclase, GGDEF domain
Domain ID domain_id1azsB00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily1230 — Nucleotide cyclase, GGDEF domain
Domain ID domain_id1azsC01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id1azsC02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology400 — GI Alpha 1, domain 2-like
Homologous superfamily homologous superfamily10 — GI Alpha 1, domain 2-like

8. Citations (1)

9. Files and Curves (10)