5mk5

Structures of DHBN domain of human BLM helicase

Method: X-RAY DIFFRACTION Dmax: 79.4 Å Quality: REASONABLE

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

Bloom syndrome protein

Homo sapiens

UniProt P54132

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 362–414 Chain B; UniProt 362–414 Fragment:UNP residues 362-414 IOD IODIDE ION × 9 K POTASSIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;298 K;Tris-HCl 0.1M pH8.5 PEG 1500 26% Glycerol 16% Resolution 2.16 Å R-free 0.297
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 362–414 Chain D; UniProt 362–414 Fragment:UNP residues 362-414 IOD IODIDE ION × 11 K POTASSIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;298 K;Tris-HCl 0.1M pH8.5 PEG 1500 26% Glycerol 16% Resolution 2.16 Å R-free 0.297

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 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BLM_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–54; UniProt 362–414 Author chain B; PDBConstruct 2–54; UniProt 362–414 Author chain C; PDBConstruct 2–54; UniProt 362–414 Author chain D; PDBConstruct 2–54; UniProt 362–414

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 5mk5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5mk5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5mk5
Deposition date deposition_date2016-12-02
Structure title titleStructures of DHBN domain of human BLM helicase
Keywords keywordshelicase dimerization alpha-helix motif, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.90
Radius of gyration Rg (electron density) rg_electron23.65
Forward intensity I(0) i016243900.00
Molecular weight molecular_weight26636.0 kDa
Excluded volume excluded_volume31115 ų
Envelope volume envelope_volume39738 ų
Hydration-shell volume shell_volume15544 ų
Envelope diameter envelope_diameter81.1
Shell Rg shell_rg28.45
Envelope Rg envelope_rg23.54
Shape Rg shape_rg23.60
Total Rg total_rg24.35
Total atoms total_atoms3481
Residues n_residues203
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 dmax79.4
Rg (real space) rg_real24.19
Rg uncertainty (real space) rg_real_error0.67
I(0) (real space) i0_real1.6240e+07
I(0) uncertainty (real space) i0_real_error2.4640e+05
Rg (reciprocal space) rg_reciprocal24.12
I(0) (reciprocal space) i0_reciprocal16240000.0000
Solution quality estimate total_estimate0.7366
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.6
Skewness Skewness skewness0.514
Kurtosis Kurtosis kurtosis-0.506
Angular range angular_range— – 0.3300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5998000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.573; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.518; Smooth: 0.336

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)