4rlv

Crystal Structure of AnkB 24 Ankyrin Repeats in Complex with AnkR Autoinhibition Segment

Method: X-RAY DIFFRACTION Dmax: 144.8 Å Quality: REASONABLE

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

Ankyrin-1, Ankyrin-2

Homo sapiens

UniProt D3YTV8

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1548–1595 Non-standard monomer:Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 9 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.6;289 K;0.5 M ammonium sulfate, 1.0 M lithium sulfate, and 0.1 M sodium citrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 3.49 Å R-free 0.253

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 D3YTV8_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 7–54; UniProt 1548–1595

Ankyrin-1, Ankyrin-2

Homo sapiens

UniProt Q01484

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 28–873 Non-standard monomer:Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 9 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.6;289 K;0.5 M ammonium sulfate, 1.0 M lithium sulfate, and 0.1 M sodium citrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 3.49 Å R-free 0.253

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.

10 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ANK2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 65–910; UniProt 28–873

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 4rlv

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4rlv
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4rlv
Deposition date deposition_date2014-10-18
Structure title titleCrystal Structure of AnkB 24 Ankyrin Repeats in Complex with AnkR Autoinhibition Segment
Keywords keywordsANK Repeat, Protein-protein interaction, Structural protein; STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier48.41
Radius of gyration Rg (electron density) rg_electron48.92
Forward intensity I(0) i0131960000.00
Molecular weight molecular_weight90720.0 kDa
Excluded volume excluded_volume112020 ų
Envelope volume envelope_volume182710 ų
Hydration-shell volume shell_volume32371 ų
Envelope diameter envelope_diameter157.1
Shell Rg shell_rg51.12
Envelope Rg envelope_rg46.49
Shape Rg shape_rg49.00
Total Rg total_rg48.75
Total atoms total_atoms6305
Residues n_residues822
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 dmax144.8
Rg (real space) rg_real48.75
Rg uncertainty (real space) rg_real_error1.22
I(0) (real space) i0_real1.3200e+08
I(0) uncertainty (real space) i0_real_error2.2000e+06
Rg (reciprocal space) rg_reciprocal48.42
I(0) (reciprocal space) i0_reciprocal131900000.0000
Solution quality estimate total_estimate0.7375
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks4
Primary peak position r_peak_primary26.3
Skewness Skewness skewness0.147
Kurtosis Kurtosis kurtosis-1.002
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2405000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.691; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.508; Smooth: 0.004

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)