5z8n

Crystal structure of Arabidopsis thaliana EBS C-terminal deletion construct in complex with an H3K4me2 peptide

Method: X-RAY DIFFRACTION Dmax: 103.0 Å Quality: EXCELLENT

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

Chromatin remodeling protein EBS

Arabidopsis thaliana

UniProt F4JL28

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 1–199 Not recorded H3K4me2 peptide × 1 (P59226) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;293 K;0.1M MES, pH 6.5, 40% PEG 200 Resolution 3.10 Å R-free 0.252
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–199 Not recorded H3K4me2 peptide × 1 (P59226) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;293 K;0.1M MES, pH 6.5, 40% PEG 200 Resolution 3.10 Å R-free 0.252
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–199 Not recorded H3K4me2 peptide × 1 (P59226) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;293 K;0.1M MES, pH 6.5, 40% PEG 200 Resolution 3.10 Å R-free 0.252

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EBS_ARATH
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–199; UniProt 1–199 Author chain B; PDBConstruct 1–199; UniProt 1–199 Author chain C; PDBConstruct 1–199; UniProt 1–199

H3K4me2 peptide

OrganismNot specified

UniProt P59226

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 2–16 Non-standard monomer:Yes (specific site not provided by mmCIF) Chromatin remodeling protein EBS × 1 (F4JL28) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;293 K;0.1M MES, pH 6.5, 40% PEG 200 Resolution 3.10 Å R-free 0.252
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain Q; UniProt 2–16 Non-standard monomer:Yes (specific site not provided by mmCIF) Chromatin remodeling protein EBS × 1 (F4JL28) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;293 K;0.1M MES, pH 6.5, 40% PEG 200 Resolution 3.10 Å R-free 0.252
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain R; UniProt 2–16 Non-standard monomer:Yes (specific site not provided by mmCIF) Chromatin remodeling protein EBS × 1 (F4JL28) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;293 K;0.1M MES, pH 6.5, 40% PEG 200 Resolution 3.10 Å R-free 0.252

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.

36 other PDB entries and 45 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H32_ARATH
Isoform
PDB entities 2
Chains and sequence ranges Author chain P; PDBConstruct 1–15; UniProt 2–16 Author chain Q; PDBConstruct 1–15; UniProt 2–16 Author chain R; PDBConstruct 1–15; UniProt 2–16

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 5z8n

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5z8n
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id5z8n
Deposition date deposition_date2018-01-31
Structure title titleCrystal structure of Arabidopsis thaliana EBS C-terminal deletion construct in complex with an H3K4me2 peptide
Keywords keywordsEBS, BAH, PHD, H3K4me2, histone reader, GENE REGULATION; GENE REGULATION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.71
Radius of gyration Rg (electron density) rg_electron31.77
Forward intensity I(0) i075994500.00
Molecular weight molecular_weight65199.0 kDa
Excluded volume excluded_volume80057 ų
Envelope volume envelope_volume117460 ų
Hydration-shell volume shell_volume31731 ų
Envelope diameter envelope_diameter105.4
Shell Rg shell_rg37.83
Envelope Rg envelope_rg30.98
Shape Rg shape_rg31.70
Total Rg total_rg32.56
Total atoms total_atoms4544
Residues n_residues564
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 dmax103.0
Rg (real space) rg_real32.64
Rg uncertainty (real space) rg_real_error0.72
I(0) (real space) i0_real7.5990e+07
I(0) uncertainty (real space) i0_real_error1.0620e+06
Rg (reciprocal space) rg_reciprocal32.68
I(0) (reciprocal space) i0_reciprocal76000000.0000
Solution quality estimate total_estimate0.9101
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary40.8
Skewness Skewness skewness0.170
Kurtosis Kurtosis kurtosis-0.622
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4361000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.965; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.939

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 5 domains

CATH v4.4 (5 domains)

Domain ID domain_id5z8nA01
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily490 — Bromo adjacent homology (BAH) domain
Domain ID domain_id5z8nA02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology40 — Herpes Virus-1
Homologous superfamily homologous superfamily10 — Zinc/RING finger domain, C3HC4 (zinc finger)
Domain ID domain_id5z8nB01
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily490 — Bromo adjacent homology (BAH) domain
Domain ID domain_id5z8nC01
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily490 — Bromo adjacent homology (BAH) domain
Domain ID domain_id5z8nC02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology40 — Herpes Virus-1
Homologous superfamily homologous superfamily10 — Zinc/RING finger domain, C3HC4 (zinc finger)

8. Citations (1)

9. Files and Curves (10)