2bnx

Crystal structure of the dimeric regulatory domain of mouse diaphaneous-related formin (DRF), mDia1

Method: X-RAY DIFFRACTION Dmax: 106.9 Å Quality: GOOD

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

DIAPHANOUS PROTEIN HOMOLOG 1

MUS MUSCULUS

UniProt O08808

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 131–516 Chain B; UniProt 131–516 Fragment:AMINO-TERMINAL DOMAIN, RESIDUES 131-516 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.25;HANGING DROP VAPOR DIFFUSION; PROTEIN: 11 MG/ML IN 100 MM HEPES, PH 7.25; RESERVOIR: 100 MM HEPES, PH 7.25, 9% PEG3350 Resolution 2.40 Å R-free 0.236

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.

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

View Construct and Data Evidence
UniProt name DIAP1_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–386; UniProt 131–516 Author chain B; PDBConstruct 1–386; UniProt 131–516

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 2bnx

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2bnx
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2bnx
Deposition date deposition_date2005-04-05
Structure title titleCrystal structure of the dimeric regulatory domain of mouse diaphaneous-related formin (DRF), mDia1
Keywords keywordsAUTOINHIBITION, ACTIN, NUCLEATION, CYTOSKELETON, 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_guinier33.44
Radius of gyration Rg (electron density) rg_electron32.76
Forward intensity I(0) i097568300.00
Molecular weight molecular_weight77297.0 kDa
Excluded volume excluded_volume96391 ų
Envelope volume envelope_volume129200 ų
Hydration-shell volume shell_volume33847 ų
Envelope diameter envelope_diameter113.0
Shell Rg shell_rg38.21
Envelope Rg envelope_rg32.56
Shape Rg shape_rg32.74
Total Rg total_rg33.26
Total atoms total_atoms5404
Residues n_residues677
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 dmax106.9
Rg (real space) rg_real33.47
Rg uncertainty (real space) rg_real_error0.87
I(0) (real space) i0_real9.7570e+07
I(0) uncertainty (real space) i0_real_error1.5040e+06
Rg (reciprocal space) rg_reciprocal33.45
I(0) (reciprocal space) i0_reciprocal97570000.0000
Solution quality estimate total_estimate0.8944
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary31.8
Skewness Skewness skewness0.261
Kurtosis Kurtosis kurtosis-0.658
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha21050000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.939; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.915; Smooth: 0.893

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2bnxa1
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.1 — ARM repeat
Family Family familya.118.1.23 — Diap1 N-terninal region-like
Domain ID domain_idd2bnxb_
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.1 — ARM repeat
Family Family familya.118.1.23 — Diap1 N-terninal region-like

CATH v4.4 (4 domains)

Domain ID domain_id2bnxA01
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily10 — Leucine-rich Repeat Variant
Domain ID domain_id2bnxA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily150 — Formin, FH3 diaphanous domain
Domain ID domain_id2bnxB01
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily10 — Leucine-rich Repeat Variant
Domain ID domain_id2bnxB02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily150 — Formin, FH3 diaphanous domain

8. Citations (1)

9. Files and Curves (10)