9vew

SIRT2 structure in complex with H3K18myr peptide and native NAD: pre-catalysis state 2

Method: X-RAY DIFFRACTION Dmax: 66.7 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 52–355 Not recorded Histone H3.1 × 1 (P68431) NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 EDO 1,2-ETHANEDIOL × 2 GOL GLYCEROL × 1 ZN ZINC ION × 1 MYR MYRISTIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289 K;Tris 8.0, 25% PEG 2000MME Resolution 2.68 Å R-free 0.251

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 1–304; UniProt 52–355

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 C; UniProt 16–22 Not recorded NAD-dependent protein deacetylase sirtuin-2 × 1 (Q8IXJ6) NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 EDO 1,2-ETHANEDIOL × 2 GOL GLYCEROL × 1 ZN ZINC ION × 1 MYR MYRISTIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289 K;Tris 8.0, 25% PEG 2000MME Resolution 2.68 Å R-free 0.251

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 C; PDBConstruct 1–7; UniProt 16–22

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 9vew

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9vew
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9vew
Deposition date deposition_date2025-06-10
Structure title titleSIRT2 structure in complex with H3K18myr peptide and native NAD: pre-catalysis state 2
Keywords keywordsdeacetylase, cell cycle regulation, metabolic regulation, hydrolase; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.68
Radius of gyration Rg (electron density) rg_electron19.51
Forward intensity I(0) i019114300.00
Molecular weight molecular_weight33337.0 kDa
Excluded volume excluded_volume41750 ų
Envelope volume envelope_volume48615 ų
Hydration-shell volume shell_volume20817 ų
Envelope diameter envelope_diameter67.8
Shell Rg shell_rg26.07
Envelope Rg envelope_rg19.87
Shape Rg shape_rg19.50
Total Rg total_rg20.43
Total atoms total_atoms2335
Residues n_residues299
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 dmax66.7
Rg (real space) rg_real20.64
Rg uncertainty (real space) rg_real_error0.47
I(0) (real space) i0_real1.9110e+07
I(0) uncertainty (real space) i0_real_error2.6180e+05
Rg (reciprocal space) rg_reciprocal20.65
I(0) (reciprocal space) i0_reciprocal19110000.0000
Solution quality estimate total_estimate0.8085
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.1
Skewness Skewness skewness0.324
Kurtosis Kurtosis kurtosis-0.266
Angular range angular_range— – 0.3850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3229000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.836; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)