7aud

Structure of an engineered helicase domain construct for human Bloom syndrome protein (BLM)

Method: X-RAY DIFFRACTION Dmax: 195.4 Å Quality: GOOD

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

Bloom syndrome protein,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–DNA Monomer Protein × 1 DNA 1 PDB declaration: protein:DNA complex(2) Consistent with all polymer counts Chain F; UniProt 636–1070 Chain F; UniProt 1202–1298 Not recorded ;DNA (5'-D(*GP*TP*AP*CP*CP*CP*GP*AP*TP*GP*TP*GP*T)-3') ; × 1 ZN ZINC ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 RY8 N-(2,3-dimethyl-5-sulfamoylphenyl)-4-(2-methylthiazol-4-yl)benzamide × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277.15 K;Morpheus HT-96, Condition C9, Molecular Dimensions. 0.09 M NPS, 0.1M Buffer System, 30% Precipitant Mix 1 NPS = 0.3 M sodium nitrate, 0.3 M sodium phosphate dibasic, 0.3 M ammonium sulphate Buffer System 1 = 1.0 M imidazole, MES monohydrate (acid) pH 6.5 60% Precipitant Mix 1 = 40% v/v PEG 500 MME, 20% w/v PEG 20000 Resolution 2.96 Å R-free 0.269
2 Protein–DNA Monomer Protein × 1 DNA 1 PDB declaration: protein:DNA complex(2) Consistent with all polymer counts Chain A; UniProt 636–1070 Chain A; UniProt 1202–1298 Not recorded ;DNA (5'-D(*GP*TP*AP*CP*CP*CP*GP*AP*TP*GP*TP*GP*T)-3') ; × 1 ZN ZINC ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 RY8 N-(2,3-dimethyl-5-sulfamoylphenyl)-4-(2-methylthiazol-4-yl)benzamide × 1 PG4 TETRAETHYLENE GLYCOL × 2 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277.15 K;Morpheus HT-96, Condition C9, Molecular Dimensions. 0.09 M NPS, 0.1M Buffer System, 30% Precipitant Mix 1 NPS = 0.3 M sodium nitrate, 0.3 M sodium phosphate dibasic, 0.3 M ammonium sulphate Buffer System 1 = 1.0 M imidazole, MES monohydrate (acid) pH 6.5 60% Precipitant Mix 1 = 40% v/v PEG 500 MME, 20% w/v PEG 20000 Resolution 2.96 Å R-free 0.269
3 Protein–DNA Monomer Protein × 1 DNA 1 PDB declaration: protein:DNA complex(2) Consistent with all polymer counts Chain B; UniProt 636–1070 Chain B; UniProt 1202–1298 Not recorded ;DNA (5'-D(*GP*TP*AP*CP*CP*CP*GP*AP*TP*GP*TP*GP*T)-3') ; × 1 ZN ZINC ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 RY8 N-(2,3-dimethyl-5-sulfamoylphenyl)-4-(2-methylthiazol-4-yl)benzamide × 1 PG4 TETRAETHYLENE GLYCOL × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277.15 K;Morpheus HT-96, Condition C9, Molecular Dimensions. 0.09 M NPS, 0.1M Buffer System, 30% Precipitant Mix 1 NPS = 0.3 M sodium nitrate, 0.3 M sodium phosphate dibasic, 0.3 M ammonium sulphate Buffer System 1 = 1.0 M imidazole, MES monohydrate (acid) pH 6.5 60% Precipitant Mix 1 = 40% v/v PEG 500 MME, 20% w/v PEG 20000 Resolution 2.96 Å R-free 0.269
4 Protein–DNA Monomer Protein × 1 DNA 1 PDB declaration: protein:DNA complex(2) Consistent with all polymer counts Chain C; UniProt 636–1070 Chain C; UniProt 1202–1298 Not recorded ;DNA (5'-D(*GP*TP*AP*CP*CP*CP*GP*AP*TP*GP*TP*GP*T)-3') ; × 1 ZN ZINC ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 RY8 N-(2,3-dimethyl-5-sulfamoylphenyl)-4-(2-methylthiazol-4-yl)benzamide × 1 PG4 TETRAETHYLENE GLYCOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277.15 K;Morpheus HT-96, Condition C9, Molecular Dimensions. 0.09 M NPS, 0.1M Buffer System, 30% Precipitant Mix 1 NPS = 0.3 M sodium nitrate, 0.3 M sodium phosphate dibasic, 0.3 M ammonium sulphate Buffer System 1 = 1.0 M imidazole, MES monohydrate (acid) pH 6.5 60% Precipitant Mix 1 = 40% v/v PEG 500 MME, 20% w/v PEG 20000 Resolution 2.96 Å R-free 0.269
5 Protein–DNA Monomer Protein × 1 DNA 1 PDB declaration: protein:DNA complex(2) Consistent with all polymer counts Chain D; UniProt 636–1070 Chain D; UniProt 1202–1298 Not recorded ;DNA (5'-D(*GP*TP*AP*CP*CP*CP*GP*AP*TP*GP*TP*GP*T)-3') ; × 1 ZN ZINC ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 RY8 N-(2,3-dimethyl-5-sulfamoylphenyl)-4-(2-methylthiazol-4-yl)benzamide × 1 PG4 TETRAETHYLENE GLYCOL × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277.15 K;Morpheus HT-96, Condition C9, Molecular Dimensions. 0.09 M NPS, 0.1M Buffer System, 30% Precipitant Mix 1 NPS = 0.3 M sodium nitrate, 0.3 M sodium phosphate dibasic, 0.3 M ammonium sulphate Buffer System 1 = 1.0 M imidazole, MES monohydrate (acid) pH 6.5 60% Precipitant Mix 1 = 40% v/v PEG 500 MME, 20% w/v PEG 20000 Resolution 2.96 Å R-free 0.269
6 Protein–DNA Monomer Protein × 1 DNA 1 PDB declaration: protein:DNA complex(2) Consistent with all polymer counts Chain E; UniProt 636–1070 Chain E; UniProt 1202–1298 Not recorded ;DNA (5'-D(*GP*TP*AP*CP*CP*CP*GP*AP*TP*GP*TP*GP*T)-3') ; × 1 ZN ZINC ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 RY8 N-(2,3-dimethyl-5-sulfamoylphenyl)-4-(2-methylthiazol-4-yl)benzamide × 1 PG4 TETRAETHYLENE GLYCOL × 1 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277.15 K;Morpheus HT-96, Condition C9, Molecular Dimensions. 0.09 M NPS, 0.1M Buffer System, 30% Precipitant Mix 1 NPS = 0.3 M sodium nitrate, 0.3 M sodium phosphate dibasic, 0.3 M ammonium sulphate Buffer System 1 = 1.0 M imidazole, MES monohydrate (acid) pH 6.5 60% Precipitant Mix 1 = 40% v/v PEG 500 MME, 20% w/v PEG 20000 Resolution 2.96 Å R-free 0.269

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 16 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 27–461; UniProt 636–1070 Author chain A; PDBConstruct 467–563; UniProt 1202–1298 Author chain B; PDBConstruct 27–461; UniProt 636–1070 Author chain B; PDBConstruct 467–563; UniProt 1202–1298 Author chain C; PDBConstruct 27–461; UniProt 636–1070 Author chain C; PDBConstruct 467–563; UniProt 1202–1298 Author chain D; PDBConstruct 27–461; UniProt 636–1070 Author chain D; PDBConstruct 467–563; UniProt 1202–1298 Author chain E; PDBConstruct 27–461; UniProt 636–1070 Author chain E; PDBConstruct 467–563; UniProt 1202–1298 Author chain F; PDBConstruct 27–461; UniProt 636–1070 Author chain F; PDBConstruct 467–563; UniProt 1202–1298

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 7aud

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7aud
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7aud
Deposition date deposition_date2020-11-02
Structure title titleStructure of an engineered helicase domain construct for human Bloom syndrome protein (BLM)
Keywords keywordsHelicase, RecQ, BLM, DNA Repair, Inhibitor, Allosteric, NUCLEAR PROTEIN; NUCLEAR PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier57.49
Radius of gyration Rg (electron density) rg_electron57.34
Forward intensity I(0) i02081720000.00
Molecular weight molecular_weight360170.0 kDa
Excluded volume excluded_volume440460 ų
Envelope volume envelope_volume705530 ų
Hydration-shell volume shell_volume101680 ų
Envelope diameter envelope_diameter214.6
Shell Rg shell_rg61.27
Envelope Rg envelope_rg55.88
Shape Rg shape_rg57.38
Total Rg total_rg57.29
Total atoms total_atoms25170
Residues n_residues3165
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 dmax195.4
Rg (real space) rg_real57.30
Rg uncertainty (real space) rg_real_error1.59
I(0) (real space) i0_real2.0820e+09
I(0) uncertainty (real space) i0_real_error4.4040e+07
Rg (reciprocal space) rg_reciprocal57.63
I(0) (reciprocal space) i0_reciprocal2083000000.0000
Solution quality estimate total_estimate0.8851
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary79.6
Skewness Skewness skewness0.130
Kurtosis Kurtosis kurtosis-0.458
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0010
Highest regularization parameter α highest_alpha86810000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.858; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.928

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (2)

9. Files and Curves (10)