5n23

Protein kinase A mutants as surrogate model for Aurora B with AT9283 inhibitor

Method: X-RAY DIFFRACTION Dmax: 67.8 Å Quality: GOOD

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

cAMP-dependent protein kinase catalytic subunit alpha

Homo sapiens

UniProt P17612

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 1–351 Mutation:K47R, L95Q, M120L, V123A, Q181K,T183A Non-standard monomer:Yes (specific site not provided by mmCIF) cAMP-dependent protein kinase inhibitor alpha × 1 (P61925) 35R 1-cyclopropyl-3-{3-[5-(morpholin-4-ylmethyl)-1H-benzimidazol-2-yl]-1H-pyrazol-4-yl}urea × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;277.15 K;12-26 % (v/v) methanol Resolution 2.09 Å R-free 0.239

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.

53 other PDB entries and 78 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KAPCA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–352; UniProt 1–351

cAMP-dependent protein kinase inhibitor alpha

OrganismNot specified

UniProt P61925

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 6–25 Not recorded cAMP-dependent protein kinase catalytic subunit alpha × 1 (P17612) 35R 1-cyclopropyl-3-{3-[5-(morpholin-4-ylmethyl)-1H-benzimidazol-2-yl]-1H-pyrazol-4-yl}urea × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;277.15 K;12-26 % (v/v) methanol Resolution 2.09 Å R-free 0.239

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.

90 other PDB entries and 100 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IPKA_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–20; UniProt 6–25

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 5n23

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5n23
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id5n23
Deposition date deposition_date2017-02-07
Structure title titleProtein kinase A mutants as surrogate model for Aurora B with AT9283 inhibitor
Keywords keywordsAT9283, Surrogate kinase, transferase; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.74
Radius of gyration Rg (electron density) rg_electron20.30
Forward intensity I(0) i028820100.00
Molecular weight molecular_weight42015.0 kDa
Excluded volume excluded_volume52913 ų
Envelope volume envelope_volume61166 ų
Hydration-shell volume shell_volume24462 ų
Envelope diameter envelope_diameter71.0
Shell Rg shell_rg27.56
Envelope Rg envelope_rg20.57
Shape Rg shape_rg20.25
Total Rg total_rg21.40
Total atoms total_atoms2970
Residues n_residues353
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 dmax67.8
Rg (real space) rg_real21.60
Rg uncertainty (real space) rg_real_error0.31
I(0) (real space) i0_real2.8820e+07
I(0) uncertainty (real space) i0_real_error3.5210e+05
Rg (reciprocal space) rg_reciprocal21.62
I(0) (reciprocal space) i0_reciprocal28820000.0000
Solution quality estimate total_estimate0.8984
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.3
Skewness Skewness skewness0.171
Kurtosis Kurtosis kurtosis-0.408
Angular range angular_range— – 0.3650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8176000.0000
Real-space data points n_real_points68
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: 0.994; Smooth: 0.989

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id5n23A01
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_id5n23A02
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)