1kna

Chromo domain of HP1 complexed with histone H3 tail containing dimethyllysine 9.

Method: X-RAY DIFFRACTION Dmax: 37.0 Å Quality: EXCELLENT

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

HETEROCHROMATIN PROTEIN 1

Drosophila melanogaster

UniProt P05205

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 17–76 Fragment:Residues 23-76 Mutation:K38M METHYLATED Histone H3 × 1 (P02299) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;283 K;Ammonium Sulfate, MES, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 283.0K Resolution 2.10 Å R-free 0.259

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.

6 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HP1_DROME
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–69; UniProt 17–76

METHYLATED Histone H3

OrganismNot specified

UniProt P02299

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 P; UniProt 1–16 Fragment:Residues 1-16 Mutation:P16Y Non-standard monomer:Yes (specific site not provided by mmCIF) HETEROCHROMATIN PROTEIN 1 × 1 (P05205) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;283 K;Ammonium Sulfate, MES, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 283.0K Resolution 2.10 Å R-free 0.259

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.

23 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H3_DROME
Isoform
PDB entities 2
Chains and sequence ranges Author chain P; PDBConstruct 1–16; UniProt 1–16

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 1kna

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1kna
Deposition date deposition_date2001-12-18
Structure title titleChromo domain of HP1 complexed with histone H3 tail containing dimethyllysine 9.
Keywords keywordschromo, HP1, histone, dimethyllysine, methyllysine, H3, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier12.25
Radius of gyration Rg (electron density) rg_electron10.81
Forward intensity I(0) i01196510.00
Molecular weight molecular_weight7082.0 kDa
Excluded volume excluded_volume8783 ų
Envelope volume envelope_volume9641 ų
Hydration-shell volume shell_volume7874 ų
Envelope diameter envelope_diameter34.1
Shell Rg shell_rg16.10
Envelope Rg envelope_rg11.14
Shape Rg shape_rg10.76
Total Rg total_rg12.31
Total atoms total_atoms499
Residues n_residues57
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 dmax37.0
Rg (real space) rg_real12.16
Rg uncertainty (real space) rg_real_error0.20
I(0) (real space) i0_real1.1970e+06
I(0) uncertainty (real space) i0_real_error1.1120e+04
Rg (reciprocal space) rg_reciprocal12.17
I(0) (reciprocal space) i0_reciprocal1197000.0000
Solution quality estimate total_estimate0.9052
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary15.9
Skewness Skewness skewness0.081
Kurtosis Kurtosis kurtosis-0.414
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha191400.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.937; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.966

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1knaa_
Class classb — All beta proteins
Fold Fold foldb.34 — SH3-like barrel
Superfamily Superfamily superfamilyb.34.13 — Chromo domain-like
Family Family familyb.34.13.2 — Chromo domain

CATH v4.4 (1 domains)

Domain ID domain_id1knaA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily40

8. Citations (1)

9. Files and Curves (10)