1qqo

E175S MUTANT OF BOVINE 70 KILODALTON HEAT SHOCK PROTEIN

Method: X-RAY DIFFRACTION Dmax: 70.5 Å Quality: GOOD

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

HYDROLASE (ACTING ON ACID ANHYDRIDES)

Bos taurus

UniProt P19120

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 4–381 Mutation:E175S MG MAGNESIUM ION × 1 CL CHLORIDE ION × 2 K POTASSIUM ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 9;277 K;POLYETHYLENE GLYCOL 8000, POTASSIUM CHLORIDE, pH 9, VAPOR DIFFUSION, HANGING DROP, temperature 4K Resolution 1.90 Å R-free 0.239

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.

41 other PDB entries and 44 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HSP7C_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–378; UniProt 4–381

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 1qqo

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1qqo
Deposition date deposition_date1999-06-07
Structure title titleE175S MUTANT OF BOVINE 70 KILODALTON HEAT SHOCK PROTEIN
Keywords keywordsHYDROLASE (ACTING ON ACID ANHYDRIDES), MOLECULAR CHAPERONE, ATPASE, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.04
Radius of gyration Rg (electron density) rg_electron21.08
Forward intensity I(0) i031036000.00
Molecular weight molecular_weight41995.0 kDa
Excluded volume excluded_volume52300 ų
Envelope volume envelope_volume61367 ų
Hydration-shell volume shell_volume24050 ų
Envelope diameter envelope_diameter73.4
Shell Rg shell_rg28.07
Envelope Rg envelope_rg21.31
Shape Rg shape_rg21.09
Total Rg total_rg21.93
Total atoms total_atoms2949
Residues n_residues378
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 dmax70.5
Rg (real space) rg_real21.92
Rg uncertainty (real space) rg_real_error0.34
I(0) (real space) i0_real3.1040e+07
I(0) uncertainty (real space) i0_real_error3.5680e+05
Rg (reciprocal space) rg_reciprocal21.94
I(0) (reciprocal space) i0_reciprocal31040000.0000
Solution quality estimate total_estimate0.8963
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.3
Skewness Skewness skewness0.202
Kurtosis Kurtosis kurtosis-0.400
Angular range angular_range— – 0.3600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8165000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.886; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.991

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1qqoa1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.55 — Ribonuclease H-like motif
Superfamily Superfamily superfamilyc.55.1 — Actin-like ATPase domain
Family Family familyc.55.1.1 — Actin/HSP70
Domain ID domain_idd1qqoa2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.55 — Ribonuclease H-like motif
Superfamily Superfamily superfamilyc.55.1 — Actin-like ATPase domain
Family Family familyc.55.1.1 — Actin/HSP70

CATH v4.4 (4 domains)

Domain ID domain_id1qqoA01
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_id1qqoA02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology30 — Defensin A-like
Homologous superfamily homologous superfamily30
Domain ID domain_id1qqoA03
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_id1qqoA04
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

8. Citations (3)

9. Files and Curves (10)