3dpp

Crystal structure of the substrate binding domain of E. coli DnaK in complex with a long pyrrhocoricin-derived inhibitor peptide (form A)

Method: X-RAY DIFFRACTION Dmax: 83.2 Å Quality: GOOD

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

Chaperone protein dnaK

Escherichia coli

UniProt P0A6Y8

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 389–607 Fragment:substrate binding domain (UNP residues 389 to 607) inhibitor peptide × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5;293 K;2.4 M ammonium sulfate, 100 mM citric acid , pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.50 Å R-free 0.316
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 389–607 Fragment:substrate binding domain (UNP residues 389 to 607) inhibitor peptide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5;293 K;2.4 M ammonium sulfate, 100 mM citric acid , pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.50 Å R-free 0.316

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.

52 other PDB entries and 124 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DNAK_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–219; UniProt 389–607 Author chain B; PDBConstruct 1–219; UniProt 389–607

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 3dpp

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3dpp
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id3dpp
Deposition date deposition_date2008-07-09
Structure title titleCrystal structure of the substrate binding domain of E. coli DnaK in complex with a long pyrrhocoricin-derived inhibitor peptide (form A)
Keywords keywords;molecular chaperone, dnaK, Hsp70, substrate-binding domain, pyrrhocoricin inhibitor, ATP-binding, Chaperone, Cytoplasm, DNA replication, Membrane, Nucleotide-binding, Phosphoprotein, Stress response, Peptide Binding Protein ;; Chaperone, Peptide Binding Protein
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.80
Radius of gyration Rg (electron density) rg_electron25.22
Forward intensity I(0) i041120200.00
Molecular weight molecular_weight48030.0 kDa
Excluded volume excluded_volume59729 ų
Envelope volume envelope_volume77769 ų
Hydration-shell volume shell_volume26734 ų
Envelope diameter envelope_diameter86.6
Shell Rg shell_rg31.19
Envelope Rg envelope_rg25.29
Shape Rg shape_rg25.21
Total Rg total_rg25.92
Total atoms total_atoms3368
Residues n_residues446
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 dmax83.2
Rg (real space) rg_real25.78
Rg uncertainty (real space) rg_real_error0.55
I(0) (real space) i0_real4.1120e+07
I(0) uncertainty (real space) i0_real_error5.7870e+05
Rg (reciprocal space) rg_reciprocal25.79
I(0) (reciprocal space) i0_reciprocal41120000.0000
Solution quality estimate total_estimate0.8992
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.9
Skewness Skewness skewness0.314
Kurtosis Kurtosis kurtosis-0.362
Angular range angular_range— – 0.3100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5651000.0000
Real-space data points n_real_points63
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.917; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.939

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id3dppA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology34 — Substrate Binding Domain Of DNAk; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Substrate Binding Domain Of DNAk; Chain A, domain 1
Domain ID domain_id3dppA02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1270 — Substrate Binding Domain Of Dnak; Chain:A; Domain 2
Homologous superfamily homologous superfamily10
Domain ID domain_id3dppB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology34 — Substrate Binding Domain Of DNAk; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Substrate Binding Domain Of DNAk; Chain A, domain 1
Domain ID domain_id3dppB02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1270 — Substrate Binding Domain Of Dnak; Chain:A; Domain 2
Homologous superfamily homologous superfamily10

8. Citations (1)

9. Files and Curves (10)