7egt

The crystal structure of the C-terminal domain of T. thermophilus UvrD complexed with the N-terminal domain of UvrB

Method: X-RAY DIFFRACTION Dmax: 118.6 Å Quality: GOOD

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

UvrABC system protein B

Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)

UniProt Q56243

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–408 Not recorded DNA helicase UvrD × 1 (O24736) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;295 K;0.1 M BIS-TRIS, pH 6.1, 15 % w/v Polyethylene glycol 1500 Resolution 2.58 Å R-free 0.249
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–408 Not recorded DNA helicase UvrD × 1 (O24736) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;295 K;0.1 M BIS-TRIS, pH 6.1, 15 % w/v Polyethylene glycol 1500 Resolution 2.58 Å R-free 0.249

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UVRB_THET8
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–411; UniProt 1–408 Author chain C; PDBConstruct 4–411; UniProt 1–408

DNA helicase UvrD

Thermus thermophilus

UniProt O24736

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 637–692 Not recorded UvrABC system protein B × 1 (Q56243) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;295 K;0.1 M BIS-TRIS, pH 6.1, 15 % w/v Polyethylene glycol 1500 Resolution 2.58 Å R-free 0.249
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 637–692 Not recorded UvrABC system protein B × 1 (Q56243) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;295 K;0.1 M BIS-TRIS, pH 6.1, 15 % w/v Polyethylene glycol 1500 Resolution 2.58 Å R-free 0.249

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name O24736_THETH
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 4–59; UniProt 637–692 Author chain D; PDBConstruct 4–59; UniProt 637–692

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 7egt

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7egt
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id7egt
Deposition date deposition_date2021-03-26
Structure title titleThe crystal structure of the C-terminal domain of T. thermophilus UvrD complexed with the N-terminal domain of UvrB
Keywords keywordsTCR, Thermus thermophilus, RNA polymerase, UvrD, UvrB, DNA repair, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier35.40
Radius of gyration Rg (electron density) rg_electron35.14
Forward intensity I(0) i0151159000.00
Molecular weight molecular_weight102110.0 kDa
Excluded volume excluded_volume129160 ų
Envelope volume envelope_volume165620 ų
Hydration-shell volume shell_volume40419 ų
Envelope diameter envelope_diameter126.6
Shell Rg shell_rg40.27
Envelope Rg envelope_rg34.84
Shape Rg shape_rg35.15
Total Rg total_rg35.48
Total atoms total_atoms7234
Residues n_residues912
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 dmax118.6
Rg (real space) rg_real35.49
Rg uncertainty (real space) rg_real_error0.97
I(0) (real space) i0_real1.5120e+08
I(0) uncertainty (real space) i0_real_error2.3520e+06
Rg (reciprocal space) rg_reciprocal35.43
I(0) (reciprocal space) i0_reciprocal151200000.0000
Solution quality estimate total_estimate0.8823
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary116.0
Skewness Skewness skewness0.382
Kurtosis Kurtosis kurtosis-0.334
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha35150000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.885; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.959; Smooth: 0.853

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)