1us7

Complex of Hsp90 and P50

Method: X-RAY DIFFRACTION Dmax: 110.9 Å Quality: REASONABLE

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

HEAT SHOCK PROTEIN HSP82

SACCHAROMYCES CEREVISIAE

UniProt P02829

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 1–214 Fragment:N-TERMINAL DOMAIN, RESIDUES 1-214 HSP90 CO-CHAPERONE CDC37 × 1 (Q16543) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;CRYSTALS OF THE COMPLEX WERE GROWN FROM A MIXTURE OF N-HSP90 AND C-P50 AT A FINAL CONCENTRATION OF 0.5MM AND 0.4MM RESPECTIVELY, IN A SOLUTION CONTAINING 12% POLYETHYLENE GLYCOL 4000, 16% ISOPROPANOL AND 100MM SODIUM CITRATE, PH 6.0. CRYSTAL DROPS WERE SET UP USING THE HANGING-DROP VAPOUR DIFFUSION METHOD, INITIALLY AT 4 DEGREES C FOR 48 HOURS AND THEN TRANSFERRED TO 14 DEGREES C. Resolution 2.30 Å R-free 0.241

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.

47 other PDB entries and 61 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HS82_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–214; UniProt 1–214

HSP90 CO-CHAPERONE CDC37

HOMO SAPIENS

UniProt Q16543

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 127–378 Fragment:C-TERMINAL DOMAIN, RESIDUES 125-378 HEAT SHOCK PROTEIN HSP82 × 1 (P02829) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;CRYSTALS OF THE COMPLEX WERE GROWN FROM A MIXTURE OF N-HSP90 AND C-P50 AT A FINAL CONCENTRATION OF 0.5MM AND 0.4MM RESPECTIVELY, IN A SOLUTION CONTAINING 12% POLYETHYLENE GLYCOL 4000, 16% ISOPROPANOL AND 100MM SODIUM CITRATE, PH 6.0. CRYSTAL DROPS WERE SET UP USING THE HANGING-DROP VAPOUR DIFFUSION METHOD, INITIALLY AT 4 DEGREES C FOR 48 HOURS AND THEN TRANSFERRED TO 14 DEGREES C. Resolution 2.30 Å R-free 0.241

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.

17 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CC37_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 14–265; UniProt 127–378

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 1us7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1us7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1us7
Deposition date deposition_date2003-11-20
Structure title titleComplex of Hsp90 and P50
Keywords keywordsCHAPERONE CO-CHAPERONE REGULATION, CHAPERONE, ATP-BINDING, HEAT SHOCK; CHAPERONE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.80
Radius of gyration Rg (electron density) rg_electron30.99
Forward intensity I(0) i034773500.00
Molecular weight molecular_weight46081.0 kDa
Excluded volume excluded_volume57894 ų
Envelope volume envelope_volume81161 ų
Hydration-shell volume shell_volume24497 ų
Envelope diameter envelope_diameter112.9
Shell Rg shell_rg33.11
Envelope Rg envelope_rg33.29
Shape Rg shape_rg30.94
Total Rg total_rg31.39
Total atoms total_atoms3238
Residues n_residues401
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 dmax110.9
Rg (real space) rg_real31.47
Rg uncertainty (real space) rg_real_error1.21
I(0) (real space) i0_real3.4770e+07
I(0) uncertainty (real space) i0_real_error5.6110e+05
Rg (reciprocal space) rg_reciprocal31.19
I(0) (reciprocal space) i0_reciprocal34770000.0000
Solution quality estimate total_estimate0.7169
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary26.1
Skewness Skewness skewness0.747
Kurtosis Kurtosis kurtosis-0.183
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3833000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.419; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.267; Smooth: 0.790

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1us7a_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.122 — ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
Superfamily Superfamily superfamilyd.122.1 — ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
Family Family familyd.122.1.1 — Heat shock protein 90, HSP90, N-terminal domain
Domain ID domain_idd1us7b_
Class classa — All alpha proteins
Fold Fold folda.205 — Hsp90 co-chaperone CDC37
Superfamily Superfamily superfamilya.205.1 — Hsp90 co-chaperone CDC37
Family Family familya.205.1.1 — Hsp90 co-chaperone CDC37

CATH v4.4 (3 domains)

Domain ID domain_id1us7A00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology565 — Heat Shock Protein 90
Homologous superfamily homologous superfamily10 — Histidine kinase-like ATPase, C-terminal domain
Domain ID domain_id1us7B01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily610 — Cdc37, Hsp90 binding domain
Domain ID domain_id1us7B02
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology140 — Helix Hairpins
Homologous superfamily homologous superfamily250

8. Citations (1)

9. Files and Curves (10)