3vu3

Crystal structure of the Hfq and catalase HPII complex

Method: X-RAY DIFFRACTION Dmax: 111.2 Å Quality: GOOD

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

Catalase HPII

OrganismNot specified

UniProt P21179

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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain A; UniProt 1–753 Not recorded Protein hfq × 24 (P0A6X3) HEM PROTOPORPHYRIN IX CONTAINING FE × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 9;293 K;0.1M Tris-HCl, 0.18M NaCl, 10% PEG4000, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.85 Å R-free 0.246

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.

46 other PDB entries and 48 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CATE_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–753; UniProt 1–753

Protein hfq

OrganismNot specified

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 heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain C; UniProt 1–102 Chain D; UniProt 1–102 Chain E; UniProt 1–102 Chain F; UniProt 1–102 Chain G; UniProt 1–102 Chain H; UniProt 1–102 Not recorded Catalase HPII × 4 (P21179) HEM PROTOPORPHYRIN IX CONTAINING FE × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 9;293 K;0.1M Tris-HCl, 0.18M NaCl, 10% PEG4000, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.85 Å R-free 0.246

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 2
Chains and sequence ranges Author chain C; PDBConstruct 1–102; UniProt 1–102 Author chain D; PDBConstruct 1–102; UniProt 1–102 Author chain E; PDBConstruct 1–102; UniProt 1–102 Author chain F; PDBConstruct 1–102; UniProt 1–102 Author chain G; PDBConstruct 1–102; UniProt 1–102 Author chain H; PDBConstruct 1–102; UniProt 1–102

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 3vu3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3vu3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3vu3
Deposition date deposition_date2012-06-15
Structure title titleCrystal structure of the Hfq and catalase HPII complex
Keywords keywordshydroperoxidase HPII, RNA binding protein, OXIDOREDUCTASE-RNA BINDING PROTEIN complex; OXIDOREDUCTASE/RNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier33.18
Radius of gyration Rg (electron density) rg_electron31.98
Forward intensity I(0) i0233750000.00
Molecular weight molecular_weight124650.0 kDa
Excluded volume excluded_volume157040 ų
Envelope volume envelope_volume203110 ų
Hydration-shell volume shell_volume51071 ų
Envelope diameter envelope_diameter120.1
Shell Rg shell_rg40.19
Envelope Rg envelope_rg32.42
Shape Rg shape_rg31.95
Total Rg total_rg32.74
Total atoms total_atoms8812
Residues n_residues1104
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 dmax111.2
Rg (real space) rg_real33.01
Rg uncertainty (real space) rg_real_error0.76
I(0) (real space) i0_real2.3370e+08
I(0) uncertainty (real space) i0_real_error3.8210e+06
Rg (reciprocal space) rg_reciprocal33.09
I(0) (reciprocal space) i0_reciprocal233800000.0000
Solution quality estimate total_estimate0.8799
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary41.7
Skewness Skewness skewness0.233
Kurtosis Kurtosis kurtosis-0.321
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha53580000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.814; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.992

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 17 domains

SCOP 2.08 (8 domains)

Domain ID domain_idd3vu3a1
Class classe — Multi-domain proteins (alpha and beta)
Fold Fold folde.5 — Heme-dependent catalase-like
Superfamily Superfamily superfamilye.5.1 — Heme-dependent catalase-like
Family Family familye.5.1.1 — Heme-dependent catalases
Domain ID domain_idd3vu3a2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.23 — Flavodoxin-like
Superfamily Superfamily superfamilyc.23.16 — Class I glutamine amidotransferase-like
Family Family familyc.23.16.3 — Catalase, C-terminal domain
Domain ID domain_idd3vu3c_
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_idd3vu3d_
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_idd3vu3e_
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_idd3vu3f_
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_idd3vu3g_
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_idd3vu3h_
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 (9 domains)

Domain ID domain_id3vu3A01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology180 — Catalase HpII, Chain A, domain 1
Homologous superfamily homologous superfamily10 — Catalase core domain
Domain ID domain_id3vu3A02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1370 — Hemocyanin, N-terminal domain
Homologous superfamily homologous superfamily20 — Catalase, four-helical domain
Domain ID domain_id3vu3A03
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily880 — Class I glutamine amidotransferase (GATase) domain
Domain ID domain_id3vu3C00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily100
Domain ID domain_id3vu3D00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily100
Domain ID domain_id3vu3E00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily100
Domain ID domain_id3vu3F00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily100
Domain ID domain_id3vu3G00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily100
Domain ID domain_id3vu3H00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily100

8. Citations (1)

9. Files and Curves (10)