1hpm

HOW POTASSIUM AFFECTS THE ACTIVITY OF THE MOLECULAR CHAPERONE HSC70. II. POTASSIUM BINDS SPECIFICALLY IN THE ATPASE ACTIVE SITE

Method: X-RAY DIFFRACTION Dmax: 70.2 Å Quality: REASONABLE

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

44K ATPASE FRAGMENT (N-TERMINAL) OF 7O kD HEAT-SHOCK COGNATE PROTEIN

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 1–386 Not recorded MG MAGNESIUM ION × 1 PO4 PHOSPHATE ION × 1 K POTASSIUM ION × 2 CL CHLORIDE ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.70 Å

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 1–386; UniProt 1–386

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 1hpm

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1hpm
Deposition date deposition_date1995-03-24
Structure title titleHOW POTASSIUM AFFECTS THE ACTIVITY OF THE MOLECULAR CHAPERONE HSC70. II. POTASSIUM BINDS SPECIFICALLY IN THE ATPASE ACTIVE SITE
Keywords keywordsHYDROLASE (ACTING ON ACID ANHYDRIDES); HYDROLASE (ACTING ON ACID ANHYDRIDES)
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.96
Radius of gyration Rg (electron density) rg_electron20.97
Forward intensity I(0) i030701100.00
Molecular weight molecular_weight41772.0 kDa
Excluded volume excluded_volume51948 ų
Envelope volume envelope_volume60766 ų
Hydration-shell volume shell_volume23913 ų
Envelope diameter envelope_diameter71.7
Shell Rg shell_rg28.07
Envelope Rg envelope_rg21.19
Shape Rg shape_rg20.99
Total Rg total_rg21.77
Total atoms total_atoms2931
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 dmax70.2
Rg (real space) rg_real21.84
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real3.0700e+07
I(0) uncertainty (real space) i0_real_error3.3970e+05
Rg (reciprocal space) rg_reciprocal21.86
I(0) (reciprocal space) i0_reciprocal30700000.0000
Solution quality estimate total_estimate0.6995
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.2
Skewness Skewness skewness0.209
Kurtosis Kurtosis kurtosis-0.399
Angular range angular_range— – 0.3600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7813000.0000
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: 0.145; Positv: 1.000; Valcen: 1.000; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1hpma1
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_idd1hpma2
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_id1hpmA01
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_id1hpmA02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology30 — Defensin A-like
Homologous superfamily homologous superfamily30
Domain ID domain_id1hpmA03
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_id1hpmA04
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 (4)

9. Files and Curves (10)