3gib

Crystal Structure of the Complex of the E. coli Hfq with Poly(A)

Method: X-RAY DIFFRACTION Dmax: 64.1 Å Quality: GOOD

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

Protein hfq

Escherichia coli

UniProt P0A6X3

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–RNA Homooligomer Protein × 6 RNA 2 PDB declaration: octameric(8) Consistent with all polymer counts Chain A; UniProt 2–69 Chain B; UniProt 2–69 Chain C; UniProt 2–69 Fragment:N-terminal fragment (2-69) 5'-R(P*AP*AP*AP*AP*AP*AP*AP*AP*A)-3' × 2 NHE 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID × 6 X-RAY DIFFRACTION X-ray crystallization conditions:pH 9.5;298 K;40% MPD, 0.1 M CHES 9.5, hanging drop, temperature 298K Resolution 2.40 Å R-free 0.259

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.

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

View Construct and Data Evidence
UniProt name HFQ_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–68; UniProt 2–69 Author chain B; PDBConstruct 1–68; UniProt 2–69 Author chain C; PDBConstruct 1–68; UniProt 2–69

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 3gib

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3gib
Deposition date deposition_date2009-03-05
Structure title titleCrystal Structure of the Complex of the E. coli Hfq with Poly(A)
Keywords keywords;RNA binding protein, Hfq-RNA complex, degradosome component, DNA-binding, RNA-binding, Stress response, RNA binding protein-RNA COMPLEX ;; RNA binding protein/RNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.25
Radius of gyration Rg (electron density) rg_electron18.16
Forward intensity I(0) i012227100.00
Molecular weight molecular_weight25135.0 kDa
Excluded volume excluded_volume31106 ų
Envelope volume envelope_volume36809 ų
Hydration-shell volume shell_volume17224 ų
Envelope diameter envelope_diameter65.5
Shell Rg shell_rg24.07
Envelope Rg envelope_rg18.62
Shape Rg shape_rg18.14
Total Rg total_rg19.08
Total atoms total_atoms1757
Residues n_residues200
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 dmax64.1
Rg (real space) rg_real19.23
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real1.2230e+07
I(0) uncertainty (real space) i0_real_error1.7130e+05
Rg (reciprocal space) rg_reciprocal19.23
I(0) (reciprocal space) i0_reciprocal12230000.0000
Solution quality estimate total_estimate0.8034
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.1
Skewness Skewness skewness0.350
Kurtosis Kurtosis kurtosis-0.185
Angular range angular_range— – 0.4150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2188000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.816; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd3giba_
Class classb — All beta proteins
Fold Fold foldb.38 — Sm-like fold
Superfamily Superfamily superfamilyb.38.1 — Sm-like ribonucleoproteins
Family Family familyb.38.1.2 — Pleiotropic translational regulator Hfq
Domain ID domain_idd3gibb_
Class classb — All beta proteins
Fold Fold foldb.38 — Sm-like fold
Superfamily Superfamily superfamilyb.38.1 — Sm-like ribonucleoproteins
Family Family familyb.38.1.2 — Pleiotropic translational regulator Hfq
Domain ID domain_idd3gibc_
Class classb — All beta proteins
Fold Fold foldb.38 — Sm-like fold
Superfamily Superfamily superfamilyb.38.1 — Sm-like ribonucleoproteins
Family Family familyb.38.1.2 — Pleiotropic translational regulator Hfq

CATH v4.4 (3 domains)

Domain ID domain_id3gibA00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily100
Domain ID domain_id3gibB00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily100
Domain ID domain_id3gibC00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily100

8. Citations (1)

9. Files and Curves (10)