8hlw

Crystal structure of SIRT3 in complex with H4K16la peptide

Method: X-RAY DIFFRACTION Dmax: 66.2 Å Quality: REASONABLE

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

NAD-dependent protein deacetylase sirtuin-3, mitochondrial

Homo sapiens

UniProt Q9NTG7

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 119–399 Not recorded Histone H4 residues 20-27 × 1 (P62805) ZN ZINC ION × 1 2OP (2S)-2-HYDROXYPROPANOIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;289 K;0.1 M Tris pH 8.5, 25% (w/v) Polyethylene glycol 3350 Resolution 2.50 Å R-free 0.243

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.

43 other PDB entries and 90 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SIR3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–281; UniProt 119–399

Histone H4 residues 20-27

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 14–21 Fragment:residues 20-27, with lactylated No.23 lysine NAD-dependent protein deacetylase sirtuin-3, mitochondrial × 1 (Q9NTG7) ZN ZINC ION × 1 2OP (2S)-2-HYDROXYPROPANOIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;289 K;0.1 M Tris pH 8.5, 25% (w/v) Polyethylene glycol 3350 Resolution 2.50 Å R-free 0.243

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 1–8; UniProt 14–21

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 8hlw

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8hlw
Deposition date deposition_date2022-12-01
Structure title titleCrystal structure of SIRT3 in complex with H4K16la peptide
Keywords keywordsSIRT3, Lysine lactylation eraser, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.52
Radius of gyration Rg (electron density) rg_electron19.22
Forward intensity I(0) i015612500.00
Molecular weight molecular_weight30522.0 kDa
Excluded volume excluded_volume38570 ų
Envelope volume envelope_volume44533 ų
Hydration-shell volume shell_volume19631 ų
Envelope diameter envelope_diameter68.7
Shell Rg shell_rg25.47
Envelope Rg envelope_rg19.35
Shape Rg shape_rg19.16
Total Rg total_rg20.30
Total atoms total_atoms4312
Residues n_residues274
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 dmax66.2
Rg (real space) rg_real20.47
Rg uncertainty (real space) rg_real_error0.45
I(0) (real space) i0_real1.5610e+07
I(0) uncertainty (real space) i0_real_error2.1440e+05
Rg (reciprocal space) rg_reciprocal20.48
I(0) (reciprocal space) i0_reciprocal15610000.0000
Solution quality estimate total_estimate0.6688
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.9
Skewness Skewness skewness0.300
Kurtosis Kurtosis kurtosis-0.303
Angular range angular_range— – 0.3850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3021000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.845; Stabil: 0.998; Sysdev: 0.387; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)