3i8d

The Pairing Geometry of the Hydrophobic Thymine Analog 2,4-Difluorotoluene in Duplex DNA as Analyzed by X-ray Crystallography

Method: X-RAY DIFFRACTION Dmax: 101.5 Å Quality: GOOD

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

Ribonuclease H

Bacillus halodurans

UniProt Q9KEI9

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 Homooligomer Protein × 2 DNA 2 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain A; UniProt 62–193 Fragment:RNase-H Mutation:D132N 5'-D(*CP*GP*CP*GP*AP*AP*TP*(DFT)P*CP*GP*CP*G)-3' × 2 GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.6;291 K;0.1 M NaOAc 3H2O (pH 4.6) and 8% (w/v) PEG 4000 , VAPOR DIFFUSION, SITTING DROP, temperature 291K Resolution 1.61 Å R-free 0.238
2 Protein–DNA Homooligomer Protein × 2 DNA 2 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain C; UniProt 62–193 Fragment:RNase-H Mutation:D132N 5'-D(*CP*GP*CP*GP*AP*AP*TP*(DFT)P*CP*GP*CP*G)-3' × 2 GOL GLYCEROL × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.6;291 K;0.1 M NaOAc 3H2O (pH 4.6) and 8% (w/v) PEG 4000 , VAPOR DIFFUSION, SITTING DROP, temperature 291K Resolution 1.61 Å R-free 0.238

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.

95 other PDB entries and 107 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RNH1_BACHD
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–132; UniProt 62–193 Author chain C; PDBConstruct 1–132; UniProt 62–193

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 3i8d

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3i8d
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3i8d
Deposition date deposition_date2009-07-09
Structure title titleThe Pairing Geometry of the Hydrophobic Thymine Analog 2,4-Difluorotoluene in Duplex DNA as Analyzed by X-ray Crystallography
Keywords keywords;RNase-H, RNase-H DNA-complex, 2, 4-Difluorotoluene, thymine isostere, hydrophobic base, Endonuclease, Hydrolase, Magnesium, Manganese, Metal-binding, Nuclease, HYDROLASE-DNA COMPLEX ;; HYDROLASE/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.24
Radius of gyration Rg (electron density) rg_electron27.56
Forward intensity I(0) i029571600.00
Molecular weight molecular_weight38126.0 kDa
Excluded volume excluded_volume46037 ų
Envelope volume envelope_volume63775 ų
Hydration-shell volume shell_volume20817 ų
Envelope diameter envelope_diameter97.3
Shell Rg shell_rg32.36
Envelope Rg envelope_rg27.41
Shape Rg shape_rg27.52
Total Rg total_rg28.19
Total atoms total_atoms2664
Residues n_residues286
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 dmax101.5
Rg (real space) rg_real28.49
Rg uncertainty (real space) rg_real_error0.95
I(0) (real space) i0_real2.9570e+07
I(0) uncertainty (real space) i0_real_error4.2800e+05
Rg (reciprocal space) rg_reciprocal28.42
I(0) (reciprocal space) i0_reciprocal29570000.0000
Solution quality estimate total_estimate0.7592
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.4
Skewness Skewness skewness0.445
Kurtosis Kurtosis kurtosis-0.460
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2376000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.754; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.604; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3i8da_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.55 — Ribonuclease H-like motif
Superfamily Superfamily superfamilyc.55.3 — Ribonuclease H-like
Family Family familyc.55.3.1 — Ribonuclease H
Domain ID domain_idd3i8dc_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.55 — Ribonuclease H-like motif
Superfamily Superfamily superfamilyc.55.3 — Ribonuclease H-like
Family Family familyc.55.3.1 — Ribonuclease H

CATH v4.4 (2 domains)

Domain ID domain_id3i8dA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily10 — Ribonuclease H-like superfamily/Ribonuclease H
Domain ID domain_id3i8dC00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily10 — Ribonuclease H-like superfamily/Ribonuclease H

8. Citations (1)

9. Files and Curves (10)