8iiz

Crystal structure of MBP fused GAS41 YEATS domain in complex with H3K27ac peptide

Method: X-RAY DIFFRACTION Dmax: 98.0 Å Quality: GOOD

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

Maltodextrin-binding protein,YEATS domain-containing protein 4

Homo sapiens

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 Heteromer Protein × 3 其他Polymer 1 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 27–392 Mutation:D108A, K109A, E198A, N199A, K265A Histone H3.1 × 2 (P68431) alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;100 mM Tris buffer (pH 8.5) containing 20% (w/v) PEG monomethyl ether 2000, 200 mM trimethylamine N-oxide Resolution 2.10 Å R-free 0.301

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 21 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 4–369; UniProt 27–392

Maltodextrin-binding protein,YEATS domain-containing protein 4

Homo sapiens

UniProt O95619

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 Heteromer Protein × 3 其他Polymer 1 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 19–159 Mutation:D108A, K109A, E198A, N199A, K265A Histone H3.1 × 2 (P68431) alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;100 mM Tris buffer (pH 8.5) containing 20% (w/v) PEG monomethyl ether 2000, 200 mM trimethylamine N-oxide Resolution 2.10 Å R-free 0.301

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.

18 other PDB entries and 42 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name YETS4_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 374–514; UniProt 19–159

Histone H3.1

OrganismNot specified

UniProt P68431

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 Heteromer Protein × 3 其他Polymer 1 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 2–33 Chain C; UniProt 2–33 Non-standard monomer:Yes (specific site not provided by mmCIF) Maltodextrin-binding protein,YEATS domain-containing protein 4 × 1 (C3SHQ8,O95619) alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;100 mM Tris buffer (pH 8.5) containing 20% (w/v) PEG monomethyl ether 2000, 200 mM trimethylamine N-oxide Resolution 2.10 Å R-free 0.301

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.

402 other PDB entries and 475 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H31_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–32; UniProt 2–33 Author chain C; PDBConstruct 1–32; UniProt 2–33

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 8iiz

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8iiz
Deposition date deposition_date2023-02-24
Structure title titleCrystal structure of MBP fused GAS41 YEATS domain in complex with H3K27ac peptide
Keywords keywordsYEATS domain, Transcription, Complex, Histone modification, NUCLEAR PROTEIN; NUCLEAR PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.84
Radius of gyration Rg (electron density) rg_electron27.19
Forward intensity I(0) i051059100.00
Molecular weight molecular_weight57927.0 kDa
Excluded volume excluded_volume73304 ų
Envelope volume envelope_volume89266 ų
Hydration-shell volume shell_volume28507 ų
Envelope diameter envelope_diameter101.8
Shell Rg shell_rg33.04
Envelope Rg envelope_rg27.38
Shape Rg shape_rg27.18
Total Rg total_rg27.84
Total atoms total_atoms4096
Residues n_residues524
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 dmax98.0
Rg (real space) rg_real27.99
Rg uncertainty (real space) rg_real_error0.90
I(0) (real space) i0_real5.1060e+07
I(0) uncertainty (real space) i0_real_error8.6640e+05
Rg (reciprocal space) rg_reciprocal27.94
I(0) (reciprocal space) i0_reciprocal51060000.0000
Solution quality estimate total_estimate0.8556
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.5
Skewness Skewness skewness0.467
Kurtosis Kurtosis kurtosis-0.270
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15110000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.758; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.863; Smooth: 0.983

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)