4j8f

Crystal structure of a fusion protein containing the NBD of Hsp70 and the middle domain of Hip

Method: X-RAY DIFFRACTION Dmax: 83.1 Å Quality: GOOD

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

Heat shock 70 kDa protein 1A/1B, Hsc70-interacting protein

Rattus norvegicus

UniProt P08107

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–382 Fragment:P08107 residues 1-382, P50503 residues 77-247 ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 2 PO4 PHOSPHATE ION × 2 IOD IODIDE ION × 34 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.4;291 K;17 % PEG-3350 and 0.2 M NH4I, pH 7.4, vapor diffusion, hanging drop, temperature 291K Resolution 2.70 Å R-free 0.261
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–382 Fragment:P08107 residues 1-382, P50503 residues 77-247 ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 PO4 PHOSPHATE ION × 1 IOD IODIDE ION × 17 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.4;291 K;17 % PEG-3350 and 0.2 M NH4I, pH 7.4, vapor diffusion, hanging drop, temperature 291K Resolution 2.70 Å R-free 0.261

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.

15 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HSP71_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 8–389; UniProt 1–382

Heat shock 70 kDa protein 1A/1B, Hsc70-interacting protein

Rattus norvegicus

UniProt P50503

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 77–247 Fragment:P08107 residues 1-382, P50503 residues 77-247 ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 2 PO4 PHOSPHATE ION × 2 IOD IODIDE ION × 34 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.4;291 K;17 % PEG-3350 and 0.2 M NH4I, pH 7.4, vapor diffusion, hanging drop, temperature 291K Resolution 2.70 Å R-free 0.261
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 77–247 Fragment:P08107 residues 1-382, P50503 residues 77-247 ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 PO4 PHOSPHATE ION × 1 IOD IODIDE ION × 17 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.4;291 K;17 % PEG-3350 and 0.2 M NH4I, pH 7.4, vapor diffusion, hanging drop, temperature 291K Resolution 2.70 Å R-free 0.261

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.

3 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name F10A1_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 391–561; UniProt 77–247

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 4j8f

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4j8f
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4j8f
Deposition date deposition_date2013-02-14
Structure title titleCrystal structure of a fusion protein containing the NBD of Hsp70 and the middle domain of Hip
Keywords keywordsactin-like fold, nucleotide binding domain, tetratricopeptide repeat, solenoid, Molecular chaperone complex, cytosol, Chaperone; CHAPERONE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.80
Radius of gyration Rg (electron density) rg_electron25.98
Forward intensity I(0) i076561000.00
Molecular weight molecular_weight62938.0 kDa
Excluded volume excluded_volume75954 ų
Envelope volume envelope_volume95620 ų
Hydration-shell volume shell_volume30957 ų
Envelope diameter envelope_diameter87.4
Shell Rg shell_rg33.20
Envelope Rg envelope_rg25.99
Shape Rg shape_rg25.97
Total Rg total_rg26.71
Total atoms total_atoms4293
Residues n_residues551
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 dmax83.1
Rg (real space) rg_real26.77
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real7.6560e+07
I(0) uncertainty (real space) i0_real_error1.1070e+06
Rg (reciprocal space) rg_reciprocal26.78
I(0) (reciprocal space) i0_reciprocal76560000.0000
Solution quality estimate total_estimate0.9000
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary81.7
Skewness Skewness skewness0.318
Kurtosis Kurtosis kurtosis-0.389
Angular range angular_range— – 0.2950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15030000.0000
Real-space data points n_real_points60
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.945; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.861

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id4j8fA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily40 — ATPase, nucleotide binding domain
Domain ID domain_id4j8fA02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily40 — ATPase, nucleotide binding domain
Domain ID domain_id4j8fA03
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology640 — Actin; Chain A, domain 4
Homologous superfamily homologous superfamily10 — ATPase, substrate binding domain, subdomain 4
Domain ID domain_id4j8fA04
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily10 — Tetratricopeptide repeat domain

8. Citations (1)

9. Files and Curves (10)