8k2r

The structure of HtpG M domain in complex with unstructured D131D binding site b

Method: SOLUTION NMR Dmax: 64.0 Å Quality: REASONABLE

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

Molecular chaperone HtpG (Fragment)

Escherichia coli

UniProt A0A7A6VTW3

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 230–494 Fragment:Heat shock protein 90 (Hsp90) M domain Disordered protein(D131D) × 1 (P00644) SOLUTION NMR NMR measurement conditions:pH 7;310 K;Ionic strength (raw mmCIF value) 150;Pressure 1 NMR sample composition:500 uM [U-100% 15N] Heat shock protein 90 (Hsp90) M domain, 500 uM [U-10% 13C; U-99% 15N] Heat shock protein 90 (Hsp90) M domain, 500 uM [U-13C; U-15N; U-2H] Heat shock protein 90 (Hsp90) M domain, 500 uM [U-100% 13C; U-100% 15N] Disordered protein (D131D), 93% H2O/7% D2O | 93% H2O/7% D2O Resolution not provided

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A7A6VTW3_ECOLX
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–268; UniProt 230–494

Disordered protein(D131D)

Staphylococcus aureus

UniProt P00644

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 152–222 Not recorded Molecular chaperone HtpG (Fragment) × 1 (A0A7A6VTW3) SOLUTION NMR NMR measurement conditions:pH 7;310 K;Ionic strength (raw mmCIF value) 150;Pressure 1 NMR sample composition:500 uM [U-100% 15N] Heat shock protein 90 (Hsp90) M domain, 500 uM [U-10% 13C; U-99% 15N] Heat shock protein 90 (Hsp90) M domain, 500 uM [U-13C; U-15N; U-2H] Heat shock protein 90 (Hsp90) M domain, 500 uM [U-100% 13C; U-100% 15N] Disordered protein (D131D), 93% H2O/7% D2O | 93% H2O/7% D2O Resolution not provided

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.

298 other PDB entries and 310 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NUC_STAAU
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 5–75; UniProt 152–222

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 8k2r

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8k2r
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8k2r
Deposition date deposition_date2023-07-13
Structure title titleThe structure of HtpG M domain in complex with unstructured D131D binding site b
Keywords keywordsE.coli Hsp90, CHAPERONE; CHAPERONE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier24.40
Radius of gyration Rg (electron density) rg_electron24.60
Forward intensity I(0) i08378660000.00
Molecular weight molecular_weight784670.0 kDa
Excluded volume excluded_volume983840 ų
Envelope volume envelope_volume194360 ų
Hydration-shell volume shell_volume47231 ų
Envelope diameter envelope_diameter119.4
Shell Rg shell_rg39.92
Envelope Rg envelope_rg37.02
Shape Rg shape_rg24.59
Total Rg total_rg24.86
Total atoms total_atoms110260
Residues n_residues6720
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 dmax64.0
Rg (real space) rg_real22.44
Rg uncertainty (real space) rg_real_error0.10
I(0) (real space) i0_real7.9000e+09
I(0) uncertainty (real space) i0_real_error7.6560e+07
Rg (reciprocal space) rg_reciprocal24.74
I(0) (reciprocal space) i0_reciprocal8378000000.0000
Solution quality estimate total_estimate0.6833
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary24.4
Skewness Skewness skewness0.367
Kurtosis Kurtosis kurtosis-0.452
Angular range angular_range— – 0.3250 −1
Current regularization parameter α current_alpha2.6010
Highest regularization parameter α highest_alpha7901000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.005; Oscil: 0.976; Stabil: 0.986; Sysdev: 0.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)