1j0r

Crystal structure of the replication termination protein mutant C110S

Method: X-RAY DIFFRACTION Dmax: 107.4 Å Quality: REASONABLE

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

replication termination protein

Bacillus subtilis

UniProt P68732

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 1–122 Mutation:C110S No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;295 K;22% PEG 2000, 150mM MES, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 2.50 Å R-free 0.279
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–122 Mutation:C110S No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;295 K;22% PEG 2000, 150mM MES, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 2.50 Å R-free 0.279

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.

6 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RTP_BACSU
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–122; UniProt 1–122 Author chain B; PDBConstruct 1–122; UniProt 1–122

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 1j0r

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1j0r
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1j0r
Deposition date deposition_date2002-11-20
Structure title titleCrystal structure of the replication termination protein mutant C110S
Keywords keywordswinged-helix, DNA-binding protein, Replication; REPLICATION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier34.97
Radius of gyration Rg (electron density) rg_electron35.13
Forward intensity I(0) i010353900.00
Molecular weight molecular_weight27397.0 kDa
Excluded volume excluded_volume35319 ų
Envelope volume envelope_volume55363 ų
Hydration-shell volume shell_volume14029 ų
Envelope diameter envelope_diameter113.4
Shell Rg shell_rg39.28
Envelope Rg envelope_rg33.45
Shape Rg shape_rg35.10
Total Rg total_rg35.64
Total atoms total_atoms1933
Residues n_residues231
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 dmax107.4
Rg (real space) rg_real35.38
Rg uncertainty (real space) rg_real_error1.18
I(0) (real space) i0_real1.0350e+07
I(0) uncertainty (real space) i0_real_error1.7290e+05
Rg (reciprocal space) rg_reciprocal35.13
I(0) (reciprocal space) i0_reciprocal10350000.0000
Solution quality estimate total_estimate0.5972
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary21.5
Skewness Skewness skewness0.271
Kurtosis Kurtosis kurtosis-1.135
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha789400.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.144; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.118; Smooth: 0.208

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1j0ra_
Class classa — All alpha proteins
Fold Fold folda.4 — DNA/RNA-binding 3-helical bundle
Superfamily Superfamily superfamilya.4.5 — 'Winged helix' DNA-binding domain
Family Family familya.4.5.7 — Replication terminator protein (RTP)
Domain ID domain_idd1j0rb_
Class classa — All alpha proteins
Fold Fold folda.4 — DNA/RNA-binding 3-helical bundle
Superfamily Superfamily superfamilya.4.5 — 'Winged helix' DNA-binding domain
Family Family familya.4.5.7 — Replication terminator protein (RTP)

CATH v4.4 (2 domains)

Domain ID domain_id1j0rA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily10 — Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain
Domain ID domain_id1j0rB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily10 — Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain

8. Citations (1)

9. Files and Curves (10)