3mh4

HtrA proteases are activated by a conserved mechanism that can be triggered by distinct molecular cues

Method: X-RAY DIFFRACTION Dmax: 108.2 Å Quality: GOOD

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

Protease do

Escherichia coli

UniProt P0C0V0

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 27–474 Mutation:S210A No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 8.5;293 K;12% Isopropanol, 0.1M Tris, 12% PEG 2000 MME, pH 8.5, VAPOR DIFFUSION, temperature 293K Resolution 3.10 Å R-free 0.309
2 Protein homooligomer Homooligomer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 27–474 Mutation:S210A No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 8.5;293 K;12% Isopropanol, 0.1M Tris, 12% PEG 2000 MME, pH 8.5, VAPOR DIFFUSION, temperature 293K Resolution 3.10 Å R-free 0.309

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 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DEGP_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–448; UniProt 27–474 Author chain B; PDBConstruct 1–448; UniProt 27–474

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 3mh4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3mh4
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id3mh4
Deposition date deposition_date2010-04-07
Structure title titleHtrA proteases are activated by a conserved mechanism that can be triggered by distinct molecular cues
Keywords keywordsDegP, HtrA, protease, Hydrolase; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.51
Radius of gyration Rg (electron density) rg_electron32.06
Forward intensity I(0) i083276700.00
Molecular weight molecular_weight71540.0 kDa
Excluded volume excluded_volume89719 ų
Envelope volume envelope_volume124800 ų
Hydration-shell volume shell_volume33396 ų
Envelope diameter envelope_diameter114.7
Shell Rg shell_rg37.53
Envelope Rg envelope_rg32.17
Shape Rg shape_rg32.04
Total Rg total_rg32.61
Total atoms total_atoms5007
Residues n_residues684
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 dmax108.2
Rg (real space) rg_real32.60
Rg uncertainty (real space) rg_real_error0.98
I(0) (real space) i0_real8.3280e+07
I(0) uncertainty (real space) i0_real_error1.3820e+06
Rg (reciprocal space) rg_reciprocal32.56
I(0) (reciprocal space) i0_reciprocal83270000.0000
Solution quality estimate total_estimate0.8892
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.8
Skewness Skewness skewness0.366
Kurtosis Kurtosis kurtosis-0.367
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14620000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.896; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.956; Smooth: 0.912

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 9 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3mh4a1
Class classb — All beta proteins
Fold Fold foldb.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamilyb.47.1 — Trypsin-like serine proteases
Family Family familyb.47.1.1 — Prokaryotic proteases
Domain ID domain_idd3mh4a2
Class classb — All beta proteins
Fold Fold foldb.36 — PDZ domain-like
Superfamily Superfamily superfamilyb.36.1 — PDZ domain-like
Family Family familyb.36.1.4 — HtrA-like serine proteases

CATH v4.4 (7 domains)

Domain ID domain_id3mh4A01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id3mh4A02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id3mh4A03
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology42 — Pdz3 Domain
Homologous superfamily homologous superfamily10 — PDZ domain
Domain ID domain_id3mh4B01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id3mh4B02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id3mh4B03
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology42 — Pdz3 Domain
Homologous superfamily homologous superfamily10 — PDZ domain
Domain ID domain_id3mh4B04
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology42 — Pdz3 Domain
Homologous superfamily homologous superfamily10 — PDZ domain

8. Citations (1)

9. Files and Curves (10)