8dei

Structure of the Cac1 KER domain

Method: X-RAY DIFFRACTION Dmax: 199.2 Å Quality: REASONABLE

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

Maltodextrin-binding protein,Chromatin assembly factor 1 subunit p90 fusion

Saccharomyces cerevisiae

UniProt C3SHQ8

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 27–392 Fragment:KER domain, residues 136-225 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;288 K;0.1 M Phosphate/citrate pH 4.2 and 30 % PEG 300 Resolution 2.81 Å R-free 0.282
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 27–392 Fragment:KER domain, residues 136-225 PEG DI(HYDROXYETHYL)ETHER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;288 K;0.1 M Phosphate/citrate pH 4.2 and 30 % PEG 300 Resolution 2.81 Å R-free 0.282
3 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 27–392 Fragment:KER domain, residues 136-225 PEG DI(HYDROXYETHYL)ETHER × 2 PO4 PHOSPHATE ION × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;288 K;0.1 M Phosphate/citrate pH 4.2 and 30 % PEG 300 Resolution 2.81 Å R-free 0.282
4 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain D; UniProt 27–392 Fragment:KER domain, residues 136-225 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;288 K;0.1 M Phosphate/citrate pH 4.2 and 30 % PEG 300 Resolution 2.81 Å R-free 0.282

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.

15 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C3SHQ8_ECOLX
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 11–376; UniProt 27–392 Author chain B; PDBConstruct 11–376; UniProt 27–392 Author chain C; PDBConstruct 11–376; UniProt 27–392 Author chain D; PDBConstruct 11–376; UniProt 27–392

Maltodextrin-binding protein,Chromatin assembly factor 1 subunit p90 fusion

Saccharomyces cerevisiae

UniProt Q12495

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 136–225 Fragment:KER domain, residues 136-225 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;288 K;0.1 M Phosphate/citrate pH 4.2 and 30 % PEG 300 Resolution 2.81 Å R-free 0.282
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 136–225 Fragment:KER domain, residues 136-225 PEG DI(HYDROXYETHYL)ETHER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;288 K;0.1 M Phosphate/citrate pH 4.2 and 30 % PEG 300 Resolution 2.81 Å R-free 0.282
3 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 136–225 Fragment:KER domain, residues 136-225 PEG DI(HYDROXYETHYL)ETHER × 2 PO4 PHOSPHATE ION × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;288 K;0.1 M Phosphate/citrate pH 4.2 and 30 % PEG 300 Resolution 2.81 Å R-free 0.282
4 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain D; UniProt 136–225 Fragment:KER domain, residues 136-225 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;288 K;0.1 M Phosphate/citrate pH 4.2 and 30 % PEG 300 Resolution 2.81 Å R-free 0.282

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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RLF2_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 401–490; UniProt 136–225 Author chain B; PDBConstruct 401–490; UniProt 136–225 Author chain C; PDBConstruct 401–490; UniProt 136–225 Author chain D; PDBConstruct 401–490; UniProt 136–225

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 8dei

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8dei
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8dei
Deposition date deposition_date2022-06-20
Structure title titleStructure of the Cac1 KER domain
Keywords keywordschromatin, DNA binding, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier74.37
Radius of gyration Rg (electron density) rg_electron75.22
Forward intensity I(0) i0584084000.00
Molecular weight molecular_weight208140.0 kDa
Excluded volume excluded_volume262420 ų
Envelope volume envelope_volume487540 ų
Hydration-shell volume shell_volume58096 ų
Envelope diameter envelope_diameter216.5
Shell Rg shell_rg64.09
Envelope Rg envelope_rg69.31
Shape Rg shape_rg75.25
Total Rg total_rg74.88
Total atoms total_atoms14746
Residues n_residues1870
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 dmax199.2
Rg (real space) rg_real74.52
Rg uncertainty (real space) rg_real_error1.27
I(0) (real space) i0_real5.8410e+08
I(0) uncertainty (real space) i0_real_error1.1600e+07
Rg (reciprocal space) rg_reciprocal73.34
I(0) (reciprocal space) i0_reciprocal582500000.0000
Solution quality estimate total_estimate0.6744
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary142.3
Skewness Skewness skewness0.054
Kurtosis Kurtosis kurtosis-1.161
Angular range angular_range— – 0.1050 −1
Current regularization parameter α current_alpha0.0004
Highest regularization parameter α highest_alpha11580000.0000
Real-space data points n_real_points22
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.522; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.201; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)