1cjk

COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE: COMPLEX WITH ADENOSINE 5'-(ALPHA THIO)-TRIPHOSPHATE (RP), MG, AND MN

Method: X-RAY DIFFRACTION Dmax: 102.4 Å Quality: GOOD

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

ADENYLATE CYCLASE, TYPE V

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 364–580 Fragment:C1A DOMAIN OF ADENYLYL CYCLASE Mutation:V476M ADENYLATE CYCLASE, TYPE II × 1 (P26769) GUANINE NUCLEOTIDE-BINDING PROTEIN G(S) × 1 (P04896) MG MAGNESIUM ION × 2 MN MANGANESE (II) ION × 1 FOK FORSKOLIN × 1 TAT ADENOSINE-5'-RP-ALPHA-THIO-TRIPHOSPHATE × 1 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 CL CHLORIDE ION × 1 GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE × 1 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 PHOSPHATE BUFFER (PH 5.4-5.6), VAPOR DIFFUSION, HANGING DROP Resolution 3.00 Å R-free 0.266

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 1–217; UniProt 364–580

ADENYLATE CYCLASE, TYPE II

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 870–1081 Fragment:C2A DOMAIN OF ADENYLYL CYCLASE ADENYLATE CYCLASE, TYPE V × 1 (P30803) GUANINE NUCLEOTIDE-BINDING PROTEIN G(S) × 1 (P04896) MG MAGNESIUM ION × 2 MN MANGANESE (II) ION × 1 FOK FORSKOLIN × 1 TAT ADENOSINE-5'-RP-ALPHA-THIO-TRIPHOSPHATE × 1 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 CL CHLORIDE ION × 1 GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE × 1 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 PHOSPHATE BUFFER (PH 5.4-5.6), VAPOR DIFFUSION, HANGING DROP Resolution 3.00 Å R-free 0.266

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

GUANINE NUCLEOTIDE-BINDING PROTEIN G(S)

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–394 Fragment:TRYPSINIZED FRAGMENT Mutation:N-TERMINAL HEXAHISTIDINE TAG ADENYLATE CYCLASE, TYPE V × 1 (P30803) ADENYLATE CYCLASE, TYPE II × 1 (P26769) MG MAGNESIUM ION × 2 MN MANGANESE (II) ION × 1 FOK FORSKOLIN × 1 TAT ADENOSINE-5'-RP-ALPHA-THIO-TRIPHOSPHATE × 1 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 CL CHLORIDE ION × 1 GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE × 1 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 PHOSPHATE BUFFER (PH 5.4-5.6), VAPOR DIFFUSION, HANGING DROP Resolution 3.00 Å R-free 0.266

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 1cjk

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1cjk
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1cjk
Deposition date deposition_date1999-04-16
Structure title titleCOMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE: COMPLEX WITH ADENOSINE 5'-(ALPHA THIO)-TRIPHOSPHATE (RP), MG, AND MN
Keywords keywordsCOMPLEX (LYASE-HYDROLASE), HYDROLASE, SIGNAL TRANSDUCING PROTEIN, CYCLASE, EFFECTOR ENZYME, LYASE-LYASE-SIGNALING PROTEIN COMPLEX; LYASE/LYASE/SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.22
Radius of gyration Rg (electron density) rg_electron31.56
Forward intensity I(0) i0111037000.00
Molecular weight molecular_weight82345.0 kDa
Excluded volume excluded_volume102470 ų
Envelope volume envelope_volume133670 ų
Hydration-shell volume shell_volume35498 ų
Envelope diameter envelope_diameter102.7
Shell Rg shell_rg38.32
Envelope Rg envelope_rg31.28
Shape Rg shape_rg31.57
Total Rg total_rg32.12
Total atoms total_atoms5765
Residues n_residues709
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 dmax102.4
Rg (real space) rg_real32.24
Rg uncertainty (real space) rg_real_error0.58
I(0) (real space) i0_real1.1100e+08
I(0) uncertainty (real space) i0_real_error1.6470e+06
Rg (reciprocal space) rg_reciprocal32.24
I(0) (reciprocal space) i0_reciprocal111000000.0000
Solution quality estimate total_estimate0.8960
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.3
Skewness Skewness skewness0.254
Kurtosis Kurtosis kurtosis-0.719
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha31530000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.923; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.966; Smooth: 0.909

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1cjka_
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_idd1cjkb_
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_idd1cjkc1
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_idd1cjkc2
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_id1cjkA00
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_id1cjkB00
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_id1cjkC01
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_id1cjkC02
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 (2)

9. Files and Curves (10)