3o7l

Crystal Structure of phospholamban (1-19):PKA C-subunit:AMP-PNP:Mg2+ complex

Method: X-RAY DIFFRACTION Dmax: 91.1 Å Quality: EXCELLENT

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

cAMP-dependent protein kinase catalytic subunit alpha

Mus musculus

UniProt P05132

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 2–351 Chain D; UniProt 2–351 Fragment:phospholamban peptide Non-standard monomer:Yes (specific site not provided by mmCIF) Non-standard monomer:Yes (specific site not provided by mmCIF) Cardiac phospholamban × 1 (P61014) MG MAGNESIUM ION × 2 PEG DI(HYDROXYETHYL)ETHER × 1 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;298 K;The complex was obtained by combining a 1:10:10:10 molar ratio mixture of PKA-C (7 mg/ml), PLN1-19, MgCl2, and AMP-PNP in 20 mM sodium acetate (pH 6.5), 180 mM KCl, and 5 mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K Resolution 2.80 Å R-free 0.287

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.

84 other PDB entries and 99 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KAPCA_MOUSE
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain B; PDBConstruct 1–350; UniProt 2–351 Author chain D; PDBConstruct 1–350; UniProt 2–351

Cardiac phospholamban

OrganismNot specified

UniProt P61014

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 I; UniProt 4–18 Not recorded cAMP-dependent protein kinase catalytic subunit alpha × 1 (P05132) cAMP-dependent protein kinase catalytic subunit alpha × 1 (P05132) MG MAGNESIUM ION × 2 PEG DI(HYDROXYETHYL)ETHER × 1 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;298 K;The complex was obtained by combining a 1:10:10:10 molar ratio mixture of PKA-C (7 mg/ml), PLN1-19, MgCl2, and AMP-PNP in 20 mM sodium acetate (pH 6.5), 180 mM KCl, and 5 mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K Resolution 2.80 Å R-free 0.287

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name PPLA_MOUSE
Isoform
PDB entities 3
Chains and sequence ranges Author chain I; PDBConstruct 1–15; UniProt 4–18

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 3o7l

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3o7l
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3o7l
Deposition date deposition_date2010-07-30
Structure title titleCrystal Structure of phospholamban (1-19):PKA C-subunit:AMP-PNP:Mg2+ complex
Keywords keywords;Protein Kinase A, Phospholamban, Allostery, Substrate Recognition, Conformational Selection, Intrinsically Disordered Proteins, Membrane Proteins, TRANSFERASE ;; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.67
Radius of gyration Rg (electron density) rg_electron27.56
Forward intensity I(0) i084251500.00
Molecular weight molecular_weight73560.0 kDa
Excluded volume excluded_volume92525 ų
Envelope volume envelope_volume114710 ų
Hydration-shell volume shell_volume34290 ų
Envelope diameter envelope_diameter91.1
Shell Rg shell_rg35.36
Envelope Rg envelope_rg27.54
Shape Rg shape_rg27.58
Total Rg total_rg28.29
Total atoms total_atoms5210
Residues n_residues674
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 dmax91.1
Rg (real space) rg_real28.61
Rg uncertainty (real space) rg_real_error0.62
I(0) (real space) i0_real8.4250e+07
I(0) uncertainty (real space) i0_real_error1.1590e+06
Rg (reciprocal space) rg_reciprocal28.64
I(0) (reciprocal space) i0_reciprocal84250000.0000
Solution quality estimate total_estimate0.9043
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary31.5
Skewness Skewness skewness0.246
Kurtosis Kurtosis kurtosis-0.540
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha21160000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.930; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.965

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3o7lb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.144 — Protein kinase-like (PK-like)
Superfamily Superfamily superfamilyd.144.1 — Protein kinase-like (PK-like)
Family Family familyd.144.1.7 — Protein kinases, catalytic subunit
Domain ID domain_idd3o7ld_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.144 — Protein kinase-like (PK-like)
Superfamily Superfamily superfamilyd.144.1 — Protein kinase-like (PK-like)
Family Family familyd.144.1.7 — Protein kinases, catalytic subunit

CATH v4.4 (4 domains)

Domain ID domain_id3o7lB01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology510 — Transferase(Phosphotransferase); domain 1
Homologous superfamily homologous superfamily10 — Transferase(Phosphotransferase) domain 1
Domain ID domain_id3o7lB02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology200 — Phosphorylase Kinase; domain 1
Homologous superfamily homologous superfamily20 — Phosphorylase Kinase; domain 1
Domain ID domain_id3o7lD01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology510 — Transferase(Phosphotransferase); domain 1
Homologous superfamily homologous superfamily10 — Transferase(Phosphotransferase) domain 1
Domain ID domain_id3o7lD02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology200 — Phosphorylase Kinase; domain 1
Homologous superfamily homologous superfamily20 — Phosphorylase Kinase; domain 1

8. Citations (1)

9. Files and Curves (10)