9nxn

Crystal structure of CN:RII alpha

Method: X-RAY DIFFRACTION Dmax: 104.5 Å Quality: GOOD

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

Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform

Homo sapiens

UniProt Q08209

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 1–370 Not recorded Calcineurin subunit B type 1 × 1 (P63098) cAMP-dependent protein kinase type II-alpha regulatory subunit × 1 (P13861) CA CALCIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5;289 K;0.1 M sodium citrate pH 5.0, 0.1 M Magnesium chloride hexahydrate, 15% PEG 4000 Resolution 2.10 Å R-free 0.250

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.

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

View Construct and Data Evidence
UniProt name PP2BA_HUMAN
Isoform Q08209-2
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–370; UniProt 1–370

Calcineurin subunit B type 1

Homo sapiens

UniProt P63098

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 1–170 Not recorded Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform × 1 (Q08209) cAMP-dependent protein kinase type II-alpha regulatory subunit × 1 (P13861) CA CALCIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5;289 K;0.1 M sodium citrate pH 5.0, 0.1 M Magnesium chloride hexahydrate, 15% PEG 4000 Resolution 2.10 Å R-free 0.250

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.

20 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CANB1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–170; UniProt 1–170

cAMP-dependent protein kinase type II-alpha regulatory subunit

Homo sapiens

UniProt P13861

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 44–103 Not recorded Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform × 1 (Q08209) Calcineurin subunit B type 1 × 1 (P63098) CA CALCIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5;289 K;0.1 M sodium citrate pH 5.0, 0.1 M Magnesium chloride hexahydrate, 15% PEG 4000 Resolution 2.10 Å R-free 0.250

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.

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

View Construct and Data Evidence
UniProt name KAP2_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 5–64; UniProt 44–103

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 9nxn

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9nxn
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9nxn
Deposition date deposition_date2025-03-25
最后修订 last_revision2025-12-17
Structure title titleCrystal structure of CN:RII alpha
Keywords keywordsCN:RII alpha, CN, RII HYDROLASE, HYDROLASE-SUBSTRATE complex, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.85
Radius of gyration Rg (electron density) rg_electron29.40
Forward intensity I(0) i056868000.00
Molecular weight molecular_weight59875.0 kDa
Excluded volume excluded_volume74993 ų
Envelope volume envelope_volume90912 ų
Hydration-shell volume shell_volume27444 ų
Envelope diameter envelope_diameter111.4
Shell Rg shell_rg34.35
Envelope Rg envelope_rg29.88
Shape Rg shape_rg29.37
Total Rg total_rg29.96
Total atoms total_atoms4208
Residues n_residues527
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 dmax104.5
Rg (real space) rg_real30.14
Rg uncertainty (real space) rg_real_error0.83
I(0) (real space) i0_real5.6870e+07
I(0) uncertainty (real space) i0_real_error8.8070e+05
Rg (reciprocal space) rg_reciprocal30.02
I(0) (reciprocal space) i0_reciprocal56860000.0000
Solution quality estimate total_estimate0.7978
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.6
Skewness Skewness skewness0.548
Kurtosis Kurtosis kurtosis-0.393
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha19700000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.600; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.655; Smooth: 0.911

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)