4e81

Crystal structure of the substrate binding domain of E.coli DnaK in complex with a short apidaecin peptide

Method: X-RAY DIFFRACTION Dmax: 80.9 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:UNP residues 389-607 apidaecin peptide fragment × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;292 K;2.7 M ammonium sulfate, 0.1 M MES, pH 6, VAPOR DIFFUSION, HANGING DROP, temperature 292K Resolution 1.90 Å R-free 0.259
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 389–607 Fragment:UNP residues 389-607 apidaecin peptide fragment × 1 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;292 K;2.7 M ammonium sulfate, 0.1 M MES, pH 6, VAPOR DIFFUSION, HANGING DROP, temperature 292K Resolution 1.90 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.

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 4e81

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4e81
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4e81
Deposition date deposition_date2012-03-19
Structure title titleCrystal structure of the substrate binding domain of E.coli DnaK in complex with a short apidaecin peptide
Keywords keywordschaperone; CHAPERONE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.86
Radius of gyration Rg (electron density) rg_electron22.95
Forward intensity I(0) i043863000.00
Molecular weight molecular_weight49142.0 kDa
Excluded volume excluded_volume60856 ų
Envelope volume envelope_volume77111 ų
Hydration-shell volume shell_volume27661 ų
Envelope diameter envelope_diameter81.3
Shell Rg shell_rg30.53
Envelope Rg envelope_rg23.22
Shape Rg shape_rg22.92
Total Rg total_rg23.90
Total atoms total_atoms3440
Residues n_residues450
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 dmax80.9
Rg (real space) rg_real23.73
Rg uncertainty (real space) rg_real_error0.49
I(0) (real space) i0_real4.3860e+07
I(0) uncertainty (real space) i0_real_error6.4380e+05
Rg (reciprocal space) rg_reciprocal23.77
I(0) (reciprocal space) i0_reciprocal43860000.0000
Solution quality estimate total_estimate0.8744
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.3
Skewness Skewness skewness0.203
Kurtosis Kurtosis kurtosis-0.386
Angular range angular_range— – 0.3350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11330000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.789; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.999

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_id4e81A01
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_id4e81A02
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_id4e81B01
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_id4e81B02
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)