1hst

CRYSTAL STRUCTURE OF GLOBULAR DOMAIN OF HISTONE H5 AND ITS IMPLICATIONS FOR NUCLEOSOME BINDING

Method: X-RAY DIFFRACTION Dmax: 57.2 Å Quality: GOOD

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

HISTONE H5

Gallus gallus

UniProt P02259

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 19–108 Not recorded No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.60 Å
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 19–108 Not recorded No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.60 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.

5 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H5_CHICK
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–90; UniProt 19–108 Author chain B; PDBConstruct 1–90; UniProt 19–108

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 1hst

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1hst
Deposition date deposition_date1993-03-30
Structure title titleCRYSTAL STRUCTURE OF GLOBULAR DOMAIN OF HISTONE H5 AND ITS IMPLICATIONS FOR NUCLEOSOME BINDING
Keywords keywordsCHROMOSOMAL PROTEIN; CHROMOSOMAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.55
Radius of gyration Rg (electron density) rg_electron16.66
Forward intensity I(0) i05041960.00
Molecular weight molecular_weight16037.0 kDa
Excluded volume excluded_volume20164 ų
Envelope volume envelope_volume24613 ų
Hydration-shell volume shell_volume12979 ų
Envelope diameter envelope_diameter61.1
Shell Rg shell_rg21.64
Envelope Rg envelope_rg16.92
Shape Rg shape_rg16.61
Total Rg total_rg17.71
Total atoms total_atoms1128
Residues n_residues148
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 dmax57.2
Rg (real space) rg_real17.54
Rg uncertainty (real space) rg_real_error0.37
I(0) (real space) i0_real5.0420e+06
I(0) uncertainty (real space) i0_real_error6.5510e+04
Rg (reciprocal space) rg_reciprocal17.54
I(0) (reciprocal space) i0_reciprocal5042000.0000
Solution quality estimate total_estimate0.8041
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary50.3
Skewness Skewness skewness0.314
Kurtosis Kurtosis kurtosis-0.432
Angular range angular_range— – 0.4550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2008000.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.828; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.967; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1hsta_
Class classa — All alpha proteins
Fold Fold folda.4 — DNA/RNA-binding 3-helical bundle
Superfamily Superfamily superfamilya.4.5 — 'Winged helix' DNA-binding domain
Family Family familya.4.5.13 — Linker histone H1/H5
Domain ID domain_idd1hstb_
Class classa — All alpha proteins
Fold Fold folda.4 — DNA/RNA-binding 3-helical bundle
Superfamily Superfamily superfamilya.4.5 — 'Winged helix' DNA-binding domain
Family Family familya.4.5.13 — Linker histone H1/H5

CATH v4.4 (2 domains)

Domain ID domain_id1hstA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily10 — Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain
Domain ID domain_id1hstB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily10 — Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain

8. Citations (2)

9. Files and Curves (10)