4tmp

Crystal structure of AF9 YEATS bound to H3K9ac peptide

Method: X-RAY DIFFRACTION Dmax: 107.9 Å Quality: REASONABLE

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

Protein AF-9

Homo sapiens

UniProt P42568

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 1–138 Fragment:YEATS domain (UNP residues 1-138) ALA-ARG-THR-LYS-GLN-THR-ALA-ARG-ALY-SER-THR × 1 (P84243) EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.6;291 K;20% PEG4000, 5% 2-Propanol, 0.1 M Sodium Citrate Tribasic Dihydrate Resolution 2.30 Å R-free 0.229
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–138 Fragment:YEATS domain (UNP residues 1-138) ALA-ARG-THR-LYS-GLN-THR-ALA-ARG-ALY-SER-THR × 1 (P84243) EDO 1,2-ETHANEDIOL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.6;291 K;20% PEG4000, 5% 2-Propanol, 0.1 M Sodium Citrate Tribasic Dihydrate Resolution 2.30 Å R-free 0.229

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.

24 other PDB entries and 37 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AF9_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–141; UniProt 1–138 Author chain C; PDBConstruct 4–141; UniProt 1–138

ALA-ARG-THR-LYS-GLN-THR-ALA-ARG-ALY-SER-THR

OrganismNot specified

UniProt P84243

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 B; UniProt 2–12 Fragment:UNP residues 2-12 Non-standard monomer:Yes (specific site not provided by mmCIF) Protein AF-9 × 1 (P42568) EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.6;291 K;20% PEG4000, 5% 2-Propanol, 0.1 M Sodium Citrate Tribasic Dihydrate Resolution 2.30 Å R-free 0.229
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 2–12 Fragment:UNP residues 2-12 Non-standard monomer:Yes (specific site not provided by mmCIF) Protein AF-9 × 1 (P42568) EDO 1,2-ETHANEDIOL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.6;291 K;20% PEG4000, 5% 2-Propanol, 0.1 M Sodium Citrate Tribasic Dihydrate Resolution 2.30 Å R-free 0.229

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.

94 other PDB entries and 122 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H33_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–11; UniProt 2–12 Author chain D; PDBConstruct 1–11; UniProt 2–12

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 4tmp

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4tmp
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4tmp
Deposition date deposition_date2014-06-02
Structure title titleCrystal structure of AF9 YEATS bound to H3K9ac peptide
Keywords keywordstranscription, complex, histone modification, immunoglobin fold; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.20
Radius of gyration Rg (electron density) rg_electron30.51
Forward intensity I(0) i019709200.00
Molecular weight molecular_weight34913.0 kDa
Excluded volume excluded_volume43948 ų
Envelope volume envelope_volume57411 ų
Hydration-shell volume shell_volume18061 ų
Envelope diameter envelope_diameter115.2
Shell Rg shell_rg32.66
Envelope Rg envelope_rg30.80
Shape Rg shape_rg30.55
Total Rg total_rg30.63
Total atoms total_atoms4908
Residues n_residues293
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 dmax107.9
Rg (real space) rg_real30.75
Rg uncertainty (real space) rg_real_error1.69
I(0) (real space) i0_real1.9710e+07
I(0) uncertainty (real space) i0_real_error3.5420e+05
Rg (reciprocal space) rg_reciprocal30.52
I(0) (reciprocal space) i0_reciprocal19710000.0000
Solution quality estimate total_estimate0.6855
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.7
Skewness Skewness skewness0.580
Kurtosis Kurtosis kurtosis-0.543
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4260000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.295; Stabil: 0.996; Sysdev: 1.000; Positv: 1.000; Valcen: 0.086; Smooth: 0.946

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id4tmpA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1970 — YEATS domain
Domain ID domain_id4tmpC00
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)