3e9f

Crystal structure short-form (residue1-113) of Eaf3 chromo domain

Method: X-RAY DIFFRACTION Dmax: 54.8 Å Quality: GOOD

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

Chromatin modification-related protein EAF3

Saccharomyces cerevisiae

UniProt Q12432

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 1–113 Fragment:Eaf3, UNP residues 1-113 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;277 K;30% polyethylene glycol 6000, 0.1M MES, pH 6.0, hanging drop, temperature 277K, VAPOR DIFFUSION, HANGING DROP Resolution 1.80 Å R-free 0.217

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.

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

View Construct and Data Evidence
UniProt name EAF3_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–113; UniProt 1–113

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 3e9f

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3e9f
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3e9f
Deposition date deposition_date2008-08-22
Structure title titleCrystal structure short-form (residue1-113) of Eaf3 chromo domain
Keywords keywords;chromatin remodeling, Eaf3, chromo domain, transcription factor, transcription regulation, Chromatin regulator, DNA damage, DNA repair, Nucleus, Transcription ;; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.56
Radius of gyration Rg (electron density) rg_electron14.36
Forward intensity I(0) i02766680.00
Molecular weight molecular_weight11791.0 kDa
Excluded volume excluded_volume14844 ų
Envelope volume envelope_volume17444 ų
Hydration-shell volume shell_volume10793 ų
Envelope diameter envelope_diameter52.9
Shell Rg shell_rg19.49
Envelope Rg envelope_rg14.95
Shape Rg shape_rg14.30
Total Rg total_rg15.67
Total atoms total_atoms830
Residues n_residues99
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 dmax54.8
Rg (real space) rg_real15.55
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real2.7670e+06
I(0) uncertainty (real space) i0_real_error3.4680e+04
Rg (reciprocal space) rg_reciprocal15.55
I(0) (reciprocal space) i0_reciprocal2767000.0000
Solution quality estimate total_estimate0.8511
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.4
Skewness Skewness skewness0.367
Kurtosis Kurtosis kurtosis-0.128
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha583000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.720; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.930; Smooth: 0.981

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id3e9fA00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily140

8. Citations (1)

9. Files and Curves (10)