1qx8

Crystal structure of a five-residue deletion mutant of the Rop protein

Method: X-RAY DIFFRACTION Dmax: 80.0 Å Quality: REASONABLE

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

Regulatory protein ROP

Escherichia coli

UniProt P03051

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–63 Chain B; UniProt 1–63 Mutation:Deletion [30D-34Q] No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.2;293 K;NaCl, methanol, Bis-Tris, DTT, EDTA, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.02 Å R-free 0.212

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.

18 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ROP_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–58; UniProt 1–63 Author chain B; PDBConstruct 1–58; UniProt 1–63

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 1qx8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1qx8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1qx8
Deposition date deposition_date2003-09-04
Structure title titleCrystal structure of a five-residue deletion mutant of the Rop protein
Keywords keywordsREPLICATION; INITIATION OF TRANSCRIPTION; RNA PRIMER; X-RAY, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.51
Radius of gyration Rg (electron density) rg_electron22.30
Forward intensity I(0) i02754280.00
Molecular weight molecular_weight11294.0 kDa
Excluded volume excluded_volume13986 ų
Envelope volume envelope_volume20875 ų
Hydration-shell volume shell_volume9543 ų
Envelope diameter envelope_diameter77.5
Shell Rg shell_rg24.97
Envelope Rg envelope_rg22.27
Shape Rg shape_rg22.29
Total Rg total_rg22.84
Total atoms total_atoms789
Residues n_residues98
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 dmax80.0
Rg (real space) rg_real22.88
Rg uncertainty (real space) rg_real_error0.83
I(0) (real space) i0_real2.7540e+06
I(0) uncertainty (real space) i0_real_error3.9960e+04
Rg (reciprocal space) rg_reciprocal22.79
I(0) (reciprocal space) i0_reciprocal2754000.0000
Solution quality estimate total_estimate0.7241
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.4
Skewness Skewness skewness0.584
Kurtosis Kurtosis kurtosis-0.288
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha144000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.355; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.485; Smooth: 0.860

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_idd1qx8a_
Class classa — All alpha proteins
Fold Fold folda.30 — ROP-like
Superfamily Superfamily superfamilya.30.1 — ROP protein
Family Family familya.30.1.1 — ROP protein
Domain ID domain_idd1qx8b_
Class classa — All alpha proteins
Fold Fold folda.30 — ROP-like
Superfamily Superfamily superfamilya.30.1 — ROP protein
Family Family familya.30.1.1 — ROP protein

CATH v4.4 (2 domains)

Domain ID domain_id1qx8A00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily1220 — Regulatory protein rop
Domain ID domain_id1qx8B00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily1220 — Regulatory protein rop

8. Citations (2)

9. Files and Curves (10)