4u68

Crystal structure of Rhino chromodomain in complex with H3K9me3

Method: X-RAY DIFFRACTION Dmax: 77.4 Å Quality: GOOD

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

Rhino

Drosophila melanogaster

UniProt Q7JXA8

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 20–90 Fragment:chromodomain, UNP residues 20-90 H3K9me3 × 2 (P02299) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;290 K;30 %(v/v) 2-methyl-2,4-pentanediol, 0.1 M sodium acetate, 25 % (w/v) PEG 1500 Resolution 1.80 Å R-free 0.206
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 20–90 Chain C; UniProt 20–90 Fragment:chromodomain, UNP residues 20-90 H3K9me3 × 2 (P02299) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;290 K;30 %(v/v) 2-methyl-2,4-pentanediol, 0.1 M sodium acetate, 25 % (w/v) PEG 1500 Resolution 1.80 Å R-free 0.206

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.

2 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q7JXA8_DROME
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–75; UniProt 20–90 Author chain B; PDBConstruct 5–75; UniProt 20–90 Author chain C; PDBConstruct 5–75; UniProt 20–90

H3K9me3

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 5–15 Non-standard monomer:Yes (specific site not provided by mmCIF) Rhino × 2 (Q7JXA8) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;290 K;30 %(v/v) 2-methyl-2,4-pentanediol, 0.1 M sodium acetate, 25 % (w/v) PEG 1500 Resolution 1.80 Å R-free 0.206
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 5–15 Chain F; UniProt 5–15 Non-standard monomer:Yes (specific site not provided by mmCIF) Rhino × 2 (Q7JXA8) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;290 K;30 %(v/v) 2-methyl-2,4-pentanediol, 0.1 M sodium acetate, 25 % (w/v) PEG 1500 Resolution 1.80 Å R-free 0.206

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 26 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 D; PDBConstruct 1–11; UniProt 5–15 Author chain E; PDBConstruct 1–11; UniProt 5–15 Author chain F; PDBConstruct 1–11; UniProt 5–15

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 4u68

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4u68
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id4u68
Deposition date deposition_date2014-07-28
Structure title titleCrystal structure of Rhino chromodomain in complex with H3K9me3
Keywords keywordsRhino, H3K9me3, piRNA, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.09
Radius of gyration Rg (electron density) rg_electron22.60
Forward intensity I(0) i09989970.00
Molecular weight molecular_weight23787.0 kDa
Excluded volume excluded_volume29941 ų
Envelope volume envelope_volume38940 ų
Hydration-shell volume shell_volume15975 ų
Envelope diameter envelope_diameter79.3
Shell Rg shell_rg27.05
Envelope Rg envelope_rg22.53
Shape Rg shape_rg22.60
Total Rg total_rg23.25
Total atoms total_atoms1678
Residues n_residues200
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 dmax77.4
Rg (real space) rg_real23.27
Rg uncertainty (real space) rg_real_error0.57
I(0) (real space) i0_real9.9900e+06
I(0) uncertainty (real space) i0_real_error1.3620e+05
Rg (reciprocal space) rg_reciprocal23.23
I(0) (reciprocal space) i0_reciprocal9990000.0000
Solution quality estimate total_estimate0.8557
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.4
Skewness Skewness skewness0.439
Kurtosis Kurtosis kurtosis-0.545
Angular range angular_range— – 0.3450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1074000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.793; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.750; Smooth: 0.991

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id4u68A00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily40
Domain ID domain_id4u68B00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily40
Domain ID domain_id4u68C00
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)