2od9

Structural Basis for Nicotinamide Inhibition and Base Exchange in Sir2 Enzymes

Method: X-RAY DIFFRACTION Dmax: 68.0 Å Quality: GOOD

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

NAD-dependent deacetylase HST2

Saccharomyces cerevisiae

UniProt P53686

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 1–294 Fragment:Hst2 catalytic core domain, residues 1-294 H4 peptide × 1 ZN ZINC ION × 1 A1R 5'-O-[(S)-{[(S)-{[(2R,3R,4S)-3,4-DIHYDROXYPYRROLIDIN-2-YL]METHOXY}(HYDROXY)PHOSPHORYL]OXY}(HYDROXY)PHOSPHORYL]ADENOSINE × 1 NCA NICOTINAMIDE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;298 K;2.0 M Ammonium Sulfate, 0.1 M sodium citrate, 0.2 M potassium/sodium tartrate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.05 Å R-free 0.245
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–294 Fragment:Hst2 catalytic core domain, residues 1-294 H4 peptide × 2 ZN ZINC ION × 2 A1R 5'-O-[(S)-{[(S)-{[(2R,3R,4S)-3,4-DIHYDROXYPYRROLIDIN-2-YL]METHOXY}(HYDROXY)PHOSPHORYL]OXY}(HYDROXY)PHOSPHORYL]ADENOSINE × 2 NCA NICOTINAMIDE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;298 K;2.0 M Ammonium Sulfate, 0.1 M sodium citrate, 0.2 M potassium/sodium tartrate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.05 Å R-free 0.245

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.

11 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HST2_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 15–308; UniProt 1–294

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 2od9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2od9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2od9
Deposition date deposition_date2006-12-21
Structure title titleStructural Basis for Nicotinamide Inhibition and Base Exchange in Sir2 Enzymes
Keywords keywordsZn binding protein, Rossmann fold, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.07
Radius of gyration Rg (electron density) rg_electron20.04
Forward intensity I(0) i019667900.00
Molecular weight molecular_weight34288.0 kDa
Excluded volume excluded_volume43123 ų
Envelope volume envelope_volume49610 ų
Hydration-shell volume shell_volume20886 ų
Envelope diameter envelope_diameter69.2
Shell Rg shell_rg26.46
Envelope Rg envelope_rg20.25
Shape Rg shape_rg19.98
Total Rg total_rg21.08
Total atoms total_atoms2411
Residues n_residues297
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 dmax68.0
Rg (real space) rg_real21.03
Rg uncertainty (real space) rg_real_error0.41
I(0) (real space) i0_real1.9670e+07
I(0) uncertainty (real space) i0_real_error2.4240e+05
Rg (reciprocal space) rg_reciprocal21.04
I(0) (reciprocal space) i0_reciprocal19670000.0000
Solution quality estimate total_estimate0.8868
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.0
Skewness Skewness skewness0.329
Kurtosis Kurtosis kurtosis-0.298
Angular range angular_range— – 0.3750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4262000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.842; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.997

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2od9a1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.31 — DHS-like NAD/FAD-binding domain
Superfamily Superfamily superfamilyc.31.1 — DHS-like NAD/FAD-binding domain
Family Family familyc.31.1.5 — Sir2 family of transcriptional regulators
Domain ID domain_idd2od9a2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id2od9A01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1220 — TPP-binding domain
Domain ID domain_id2od9A02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1600 — SIR2/SIRT2 'Small Domain'
Homologous superfamily homologous superfamily10 — SIR2/SIRT2 'Small Domain'

8. Citations (1)

9. Files and Curves (10)