5xtz

Crystal structure of GAS41 YEATS bound to H3K27ac peptide

Method: X-RAY DIFFRACTION Dmax: 119.1 Å Quality: GOOD

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

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 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 15–159 Chain B; UniProt 15–159 Chain C; UniProt 15–159 Chain D; UniProt 15–159 Fragment:UNP RESIDUES 15-159 THR-LYS-ALA-ALA-ARG-ALY-SER-ALA-PRO-ALA × 1 ACT ACETATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.6;291 K;0.1 M sodium acetate trihydrate, pH 4.6, 4.0 M ammonium acetate Resolution 2.10 Å R-free 0.233
2 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 15–159 Chain B; UniProt 15–159 Chain C; UniProt 15–159 Chain D; UniProt 15–159 Fragment:UNP RESIDUES 15-159 THR-LYS-ALA-ALA-ARG-ALY-SER-ALA-PRO-ALA × 1 ACT ACETATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.6;291 K;0.1 M sodium acetate trihydrate, pH 4.6, 4.0 M ammonium acetate Resolution 2.10 Å R-free 0.233

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 41 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 19–163; UniProt 15–159 Author chain B; PDBConstruct 19–163; UniProt 15–159 Author chain C; PDBConstruct 19–163; UniProt 15–159 Author chain D; PDBConstruct 19–163; UniProt 15–159

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 5xtz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5xtz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5xtz
Deposition date deposition_date2017-06-21
Structure title titleCrystal structure of GAS41 YEATS bound to H3K27ac peptide
Keywords keywordsepigenetic, histone acetylation, 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_guinier34.55
Radius of gyration Rg (electron density) rg_electron34.38
Forward intensity I(0) i064125100.00
Molecular weight molecular_weight66742.0 kDa
Excluded volume excluded_volume84939 ų
Envelope volume envelope_volume119570 ų
Hydration-shell volume shell_volume31017 ų
Envelope diameter envelope_diameter123.3
Shell Rg shell_rg38.06
Envelope Rg envelope_rg34.01
Shape Rg shape_rg34.30
Total Rg total_rg35.00
Total atoms total_atoms4720
Residues n_residues569
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 dmax119.1
Rg (real space) rg_real34.77
Rg uncertainty (real space) rg_real_error1.21
I(0) (real space) i0_real6.4130e+07
I(0) uncertainty (real space) i0_real_error1.1010e+06
Rg (reciprocal space) rg_reciprocal34.64
I(0) (reciprocal space) i0_reciprocal64120000.0000
Solution quality estimate total_estimate0.7995
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary36.2
Skewness Skewness skewness0.448
Kurtosis Kurtosis kurtosis-0.381
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4779000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.841; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.868; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id5xtzA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1970 — YEATS domain
Domain ID domain_id5xtzB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1970 — YEATS domain
Domain ID domain_id5xtzC00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1970 — YEATS domain
Domain ID domain_id5xtzD00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1970 — YEATS domain

8. Citations (1)

9. Files and Curves (10)