6m3q

Crystal structure of AnkB/beta4-spectrin complex

Method: X-RAY DIFFRACTION Dmax: 139.5 Å Quality: GOOD

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

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 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 951–1458 Not recorded Spectrin beta chain × 1 (Q8VIE5) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.5;289 K;25% w/v pentaerythritol propoxylate 629 (17/8 PO/OH), 50 mM magnesium chloride and 0.1 M HEPES, pH 7.5 Resolution 3.44 Å R-free 0.307

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 E; PDBConstruct 1–475; UniProt 951–1458

Spectrin beta chain

Mus musculus

UniProt Q8VIE5

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 F; UniProt 1616–1937 Not recorded Ankyrin-2 × 1 (Q01484) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.5;289 K;25% w/v pentaerythritol propoxylate 629 (17/8 PO/OH), 50 mM magnesium chloride and 0.1 M HEPES, pH 7.5 Resolution 3.44 Å R-free 0.307

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q8VIE5_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain F; PDBConstruct 1–322; UniProt 1616–1937

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 6m3q

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6m3q
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6m3q
Deposition date deposition_date2020-03-04
Structure title titleCrystal structure of AnkB/beta4-spectrin complex
Keywords keywordsPROTEIN BINDING, 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_guinier37.05
Radius of gyration Rg (electron density) rg_electron37.24
Forward intensity I(0) i095031400.00
Molecular weight molecular_weight77313.0 kDa
Excluded volume excluded_volume96549 ų
Envelope volume envelope_volume135900 ų
Hydration-shell volume shell_volume33834 ų
Envelope diameter envelope_diameter147.2
Shell Rg shell_rg38.30
Envelope Rg envelope_rg37.97
Shape Rg shape_rg37.30
Total Rg total_rg37.13
Total atoms total_atoms5445
Residues n_residues754
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 dmax139.5
Rg (real space) rg_real37.41
Rg uncertainty (real space) rg_real_error1.34
I(0) (real space) i0_real9.5030e+07
I(0) uncertainty (real space) i0_real_error1.6800e+06
Rg (reciprocal space) rg_reciprocal37.19
I(0) (reciprocal space) i0_reciprocal95010000.0000
Solution quality estimate total_estimate0.8161
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary42.2
Skewness Skewness skewness0.540
Kurtosis Kurtosis kurtosis-0.090
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7954000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.682; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.578; Smooth: 0.982

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id6m3qE01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology220 — Chondroitinase Ac; Chain A, domain 3
Homologous superfamily homologous superfamily30
Domain ID domain_id6m3qE02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology220 — Chondroitinase Ac; Chain A, domain 3
Homologous superfamily homologous superfamily30
Domain ID domain_id6m3qE03
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily2660
Domain ID domain_id6m3qF00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily60

8. Citations (1)

9. Files and Curves (10)