8tgp

Crystal structure of SIRT2 with FAM-PEG4-H4K16(myristoyl) peptide

Method: X-RAY DIFFRACTION Dmax: 69.2 Å Quality: GOOD

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

NAD-dependent protein deacetylase sirtuin-2

Homo sapiens

UniProt Q8IXJ6

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 34–356 Not recorded H4K16(myristoyl) peptide × 1 (P62805) ZN ZINC ION × 1 MYR MYRISTIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;293 K;0.2 M MES monohydrate pH 6.5 (NaOH), 20% w/v PEG 4,000 Resolution 1.76 Å R-free 0.230

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.

77 other PDB entries and 97 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SIR2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–323; UniProt 34–356

H4K16(myristoyl) peptide

OrganismNot specified

UniProt P62805

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 9–21 Not recorded NAD-dependent protein deacetylase sirtuin-2 × 1 (Q8IXJ6) ZN ZINC ION × 1 MYR MYRISTIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;293 K;0.2 M MES monohydrate pH 6.5 (NaOH), 20% w/v PEG 4,000 Resolution 1.76 Å R-free 0.230

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.

581 other PDB entries and 633 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H4_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–13; UniProt 9–21

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 8tgp

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8tgp
Deposition date deposition_date2023-07-12
Structure title titleCrystal structure of SIRT2 with FAM-PEG4-H4K16(myristoyl) peptide
Keywords keywordsSirtuin Sirtuin-2 SIRT2, GENE REGULATION, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.84
Radius of gyration Rg (electron density) rg_electron19.72
Forward intensity I(0) i017262200.00
Molecular weight molecular_weight32165.0 kDa
Excluded volume excluded_volume40584 ų
Envelope volume envelope_volume47265 ų
Hydration-shell volume shell_volume20319 ų
Envelope diameter envelope_diameter71.5
Shell Rg shell_rg26.00
Envelope Rg envelope_rg19.93
Shape Rg shape_rg19.71
Total Rg total_rg20.67
Total atoms total_atoms2256
Residues n_residues281
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 dmax69.2
Rg (real space) rg_real20.81
Rg uncertainty (real space) rg_real_error0.42
I(0) (real space) i0_real1.7260e+07
I(0) uncertainty (real space) i0_real_error2.2200e+05
Rg (reciprocal space) rg_reciprocal20.82
I(0) (reciprocal space) i0_reciprocal17260000.0000
Solution quality estimate total_estimate0.8802
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.1
Skewness Skewness skewness0.329
Kurtosis Kurtosis kurtosis-0.298
Angular range angular_range— – 0.3800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2801000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.824; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.968

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)