2rc4

Crystal Structure of the HAT domain of the human MOZ protein

Method: X-RAY DIFFRACTION Dmax: 70.7 Å Quality: REASONABLE

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

Histone acetyltransferase MYST3

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 501–784 Fragment:HAT domain ZN ZINC ION × 1 ACO ACETYL COENZYME *A × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 6.5;298 K;sodium cacodylate, PEG 3350, pH 6.5, VAPOR DIFFUSION, temperature 298K Resolution 3.00 Å R-free 0.283

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 MYST3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–284; UniProt 501–784

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 2rc4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2rc4
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id2rc4
Deposition date deposition_date2007-09-19
Structure title titleCrystal Structure of the HAT domain of the human MOZ protein
Keywords keywords;Coenzyme A binding domain, zinc-finger, helix-turn-helix, Activator, Acyltransferase, Chromatin regulator, Metal-binding, Nucleus, Phosphorylation, Proto-oncogene, Repressor, Transcription, Transcription regulation, Transferase ;; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.61
Radius of gyration Rg (electron density) rg_electron19.61
Forward intensity I(0) i016829900.00
Molecular weight molecular_weight30606.0 kDa
Excluded volume excluded_volume38173 ų
Envelope volume envelope_volume45802 ų
Hydration-shell volume shell_volume19868 ų
Envelope diameter envelope_diameter72.6
Shell Rg shell_rg25.90
Envelope Rg envelope_rg20.14
Shape Rg shape_rg19.58
Total Rg total_rg20.63
Total atoms total_atoms2145
Residues n_residues264
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 dmax70.7
Rg (real space) rg_real20.62
Rg uncertainty (real space) rg_real_error0.53
I(0) (real space) i0_real1.6830e+07
I(0) uncertainty (real space) i0_real_error2.2810e+05
Rg (reciprocal space) rg_reciprocal20.62
I(0) (reciprocal space) i0_reciprocal16830000.0000
Solution quality estimate total_estimate0.6384
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary24.6
Skewness Skewness skewness0.447
Kurtosis Kurtosis kurtosis-0.044
Angular range angular_range— – 0.3850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3943000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.717; Stabil: 0.999; Sysdev: 0.387; Positv: 1.000; Valcen: 0.986; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2rc4a1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.108 — Acyl-CoA N-acyltransferases (Nat)
Superfamily Superfamily superfamilyd.108.1 — Acyl-CoA N-acyltransferases (Nat)
Family Family familyd.108.1.1 — N-acetyl transferase, NAT

CATH v4.4 (3 domains)

Domain ID domain_id2rc4A01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology60 — Wheat Germ Agglutinin (Isolectin 2); domain 1
Homologous superfamily homologous superfamily60 — N-acetyl transferase-like
Domain ID domain_id2rc4A02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology630 — Aminopeptidase
Homologous superfamily homologous superfamily30 — Gcn5-related N-acetyltransferase (GNAT)
Domain ID domain_id2rc4A03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily10 — Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain

8. Citations (1)

9. Files and Curves (10)