3fhi

Crystal structure of a complex between the catalytic and regulatory (RI{alpha}) subunits of PKA

Method: X-RAY DIFFRACTION Dmax: 79.7 Å Quality: GOOD

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 2–351 Mutation:C199A Non-standard monomer:Yes (specific site not provided by mmCIF) cAMP-dependent protein kinase type I-alpha regulatory subunit × 1 (P00514) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;20 % PEG 2000, 0.1 M Tris-HCl, 4 % 1,3-Propanediol, 2.0 mM Cyclohexyl-pentyl-D-maltoside, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.00 Å R-free 0.226

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
Chains and sequence ranges Author chain A; PDBConstruct 1–350; UniProt 2–351

cAMP-dependent protein kinase type I-alpha regulatory subunit

Bos taurus

UniProt P00514

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 92–245 Fragment:UNP residues 92-245 cAMP-dependent protein kinase catalytic subunit alpha × 1 (P05132) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;20 % PEG 2000, 0.1 M Tris-HCl, 4 % 1,3-Propanediol, 2.0 mM Cyclohexyl-pentyl-D-maltoside, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.00 Å R-free 0.226

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.

25 other PDB entries and 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KAP0_BOVIN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–154; UniProt 92–245

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 3fhi

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3fhi
Deposition date deposition_date2008-12-09
Structure title titleCrystal structure of a complex between the catalytic and regulatory (RI{alpha}) subunits of PKA
Keywords keywords;cAMP, cAMP dependent protein kinase, Protein-Protein complex, AMP-PNP, Protein kinase Regulation, nucleotide binding, protein kinase activity, protein serine/threonine kinase activity, cAMP-dependent protein kinase activity, protein binding, ATP binding, kinase activity, transferase activity, ATP-binding, Kinase, Lipoprotein, Myristate, Nucleotide-binding, Nucleus, Phosphoprotein, Serine/threonine-protein kinase, Transferase, cAMP-binding ;; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.69
Radius of gyration Rg (electron density) rg_electron23.63
Forward intensity I(0) i048972800.00
Molecular weight molecular_weight54939.0 kDa
Excluded volume excluded_volume68974 ų
Envelope volume envelope_volume81032 ų
Hydration-shell volume shell_volume28295 ų
Envelope diameter envelope_diameter79.6
Shell Rg shell_rg30.99
Envelope Rg envelope_rg23.87
Shape Rg shape_rg23.64
Total Rg total_rg24.45
Total atoms total_atoms3875
Residues n_residues486
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 dmax79.7
Rg (real space) rg_real24.59
Rg uncertainty (real space) rg_real_error0.54
I(0) (real space) i0_real4.8970e+07
I(0) uncertainty (real space) i0_real_error7.1870e+05
Rg (reciprocal space) rg_reciprocal24.62
I(0) (reciprocal space) i0_reciprocal48970000.0000
Solution quality estimate total_estimate0.8985
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary29.1
Skewness Skewness skewness0.231
Kurtosis Kurtosis kurtosis-0.455
Angular range angular_range— – 0.3200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9530000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.897; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.987

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3fhia_
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 (3 domains)

Domain ID domain_id3fhiA01
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_id3fhiA02
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_id3fhiB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily10 — Jelly Rolls

8. Citations (1)

9. Files and Curves (10)