3v43

Crystal structure of MOZ

Method: X-RAY DIFFRACTION Dmax: 53.4 Å Quality: GOOD

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

Histone acetyltransferase KAT6A

Homo sapiens

UniProt Q92794

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 204–313 Fragment:UNP RESIDUES 204-313 Histone H3.1 × 1 (P68431) ZN ZINC ION × 4 ACT ACETATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.6;293 K;0.2M ammonium acetate, 0.1M tri-sodium citrate, 30% w/v PEG 4000, pH 5.6, vapor diffusion, hanging drop, temperature 293K Resolution 1.47 Å R-free 0.176

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.

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

View Construct and Data Evidence
UniProt name KAT6A_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–112; UniProt 204–313

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 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain Q; UniProt 2–19 Fragment:UNP RESIDUES 2-19 Non-standard monomer:Yes (specific site not provided by mmCIF) Histone acetyltransferase KAT6A × 1 (Q92794) ZN ZINC ION × 4 ACT ACETATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.6;293 K;0.2M ammonium acetate, 0.1M tri-sodium citrate, 30% w/v PEG 4000, pH 5.6, vapor diffusion, hanging drop, temperature 293K Resolution 1.47 Å R-free 0.176

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 Q; PDBConstruct 1–18; UniProt 2–19

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 3v43

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3v43
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3v43
Deposition date deposition_date2011-12-14
Structure title titleCrystal structure of MOZ
Keywords keywordsMOZ, PHD finger, Histone H3, TRANSFERASE-STRUCTURAL PROTEIN complex; TRANSFERASE/STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.37
Radius of gyration Rg (electron density) rg_electron14.71
Forward intensity I(0) i04487260.00
Molecular weight molecular_weight13601.0 kDa
Excluded volume excluded_volume16346 ų
Envelope volume envelope_volume19219 ų
Hydration-shell volume shell_volume11511 ų
Envelope diameter envelope_diameter52.1
Shell Rg shell_rg19.71
Envelope Rg envelope_rg15.07
Shape Rg shape_rg14.73
Total Rg total_rg15.60
Total atoms total_atoms921
Residues n_residues119
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 dmax53.4
Rg (real space) rg_real15.35
Rg uncertainty (real space) rg_real_error0.47
I(0) (real space) i0_real4.4870e+06
I(0) uncertainty (real space) i0_real_error5.5740e+04
Rg (reciprocal space) rg_reciprocal15.36
I(0) (reciprocal space) i0_reciprocal4487000.0000
Solution quality estimate total_estimate0.8693
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.6
Skewness Skewness skewness0.315
Kurtosis Kurtosis kurtosis-0.271
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha511600.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.789; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.948; Smooth: 0.981

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id3v43A00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology40 — Herpes Virus-1
Homologous superfamily homologous superfamily10 — Zinc/RING finger domain, C3HC4 (zinc finger)

8. Citations (1)

9. Files and Curves (10)