7c0j

Crystal structure of chimeric mutant of GH5 in complex with Z-DNA

Method: X-RAY DIFFRACTION Dmax: 52.3 Å Quality: REASONABLE

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

Histone H5,Double-stranded RNA-specific adenosine deaminase

Gallus gallus

UniProt P02259

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 Homooligomer Protein × 2 DNA 2 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain A; UniProt 25–64 Chain A; UniProt 76–88 Chain A; UniProt 92–93 Chain A; UniProt 95–98 Chain B; UniProt 25–64 Chain B; UniProt 76–88 Chain B; UniProt 92–93 Chain B; UniProt 95–98 Mutation:K41G,S42E,R43G,K53A,R95A ;DNA (5'-D(*TP*CP*GP*CP*GP*CP*G)-3') ; × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;295 K;MES pH 6.0, PEG 4000, ethylene glycol Resolution 2.75 Å R-free 0.248

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.

5 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H5_CHICK
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–45; UniProt 25–64 Author chain A; PDBConstruct 56–68; UniProt 76–88 Author chain A; PDBConstruct 70–71; UniProt 92–93 Author chain A; PDBConstruct 73–76; UniProt 95–98 Author chain B; PDBConstruct 6–45; UniProt 25–64 Author chain B; PDBConstruct 56–68; UniProt 76–88 Author chain B; PDBConstruct 70–71; UniProt 92–93 Author chain B; PDBConstruct 73–76; UniProt 95–98

Histone H5,Double-stranded RNA-specific adenosine deaminase

Gallus gallus

UniProt P55265

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 Homooligomer Protein × 2 DNA 2 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain A; UniProt 169–178 Chain A; UniProt 192–192 Chain A; UniProt 195–195 Chain B; UniProt 169–178 Chain B; UniProt 192–192 Chain B; UniProt 195–195 Mutation:K41G,S42E,R43G,K53A,R95A ;DNA (5'-D(*TP*CP*GP*CP*GP*CP*G)-3') ; × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;295 K;MES pH 6.0, PEG 4000, ethylene glycol Resolution 2.75 Å R-free 0.248

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.

23 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DSRAD_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 46–55; UniProt 169–178 Author chain A; PDBConstruct 69–69; UniProt 192–192 Author chain A; PDBConstruct 72–72; UniProt 195–195 Author chain B; PDBConstruct 46–55; UniProt 169–178 Author chain B; PDBConstruct 69–69; UniProt 192–192 Author chain B; PDBConstruct 72–72; UniProt 195–195

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 7c0j

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7c0j
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7c0j
Deposition date deposition_date2020-05-01
Structure title titleCrystal structure of chimeric mutant of GH5 in complex with Z-DNA
Keywords keywordsGH5, Protein-DNA complex, protein engineering, Z-DNA binding protein, DNA BINDING PROTEIN, DNA BINDING PROTEIN-DNA complex; DNA BINDING PROTEIN/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.35
Radius of gyration Rg (electron density) rg_electron19.01
Forward intensity I(0) i06683840.00
Molecular weight molecular_weight16810.0 kDa
Excluded volume excluded_volume20104 ų
Envelope volume envelope_volume25142 ų
Hydration-shell volume shell_volume12352 ų
Envelope diameter envelope_diameter63.0
Shell Rg shell_rg22.88
Envelope Rg envelope_rg19.27
Shape Rg shape_rg19.06
Total Rg total_rg19.46
Total atoms total_atoms1169
Residues n_residues133
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 dmax52.3
Rg (real space) rg_real17.57
Rg uncertainty (real space) rg_real_error0.11
I(0) (real space) i0_real6.4400e+06
I(0) uncertainty (real space) i0_real_error5.3970e+04
Rg (reciprocal space) rg_reciprocal18.53
I(0) (reciprocal space) i0_reciprocal6684000.0000
Solution quality estimate total_estimate0.6678
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary17.7
Skewness Skewness skewness0.521
Kurtosis Kurtosis kurtosis-0.244
Angular range angular_range— – 0.4350 −1
Current regularization parameter α current_alpha3.5730
Highest regularization parameter α highest_alpha1196000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.915; Stabil: 0.987; Sysdev: 0.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)