3glu

Crystal Structure of Human SIRT3 with AceCS2 peptide

Method: X-RAY DIFFRACTION
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1. Protein Identity and Related Structures Protein Identity & Related Structures

NAD-dependent deacetylase sirtuin-3, mitochondrial

Homo sapiens

UniProt Q9NTG7

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 4 Acetyl-coenzyme A synthetase 2-like, mitochondrial × 2 (Q9NUB1) SULFATE ION × 4 ZINC ION × 2 water × 4 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name SIRT3_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–285; UniProt 118–399

Acetyl-coenzyme A synthetase 2-like, mitochondrial

OrganismNot specified

UniProt Q9NUB1

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 4 NAD-dependent deacetylase sirtuin-3, mitochondrial × 2 (Q9NTG7) SULFATE ION × 4 ZINC ION × 2 water × 4 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name ACS2L_HUMAN
Isoform —
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–12; UniProt 638–649

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id3glu
Deposition date deposition_date2009-03-12
Structure title titleCrystal Structure of Human SIRT3 with AceCS2 peptide
Keywords keywords;NAD dependent deacetylase, sirtuin, product peptide complex, Hydrolase, Metal-binding, Mitochondrion, NAD, Polymorphism, Transit peptide, Zinc, Alternative splicing, Ligase, HYDROLASE-HYDROLASE REGULATOR COMPLEX ;; HYDROLASE/HYDROLASE REGULATOR
Experimental Method methodX-RAY DIFFRACTION
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

3glu__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

3glu__assembly_1__model_1 | I(q)

10-2 10-1 106 107 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

3glu__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)29.04 Å
Rg (electron density)27.82 Å
Total Rg28.63 Å
Atom count4366
Residues554
Excluded volume78406 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 3glu__assembly_1__model_1 tetrameric (4) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (5)

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6. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id3gluA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1220 — TPP-binding domain
Domain ID domain_id3gluA02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1600 — SIR2/SIRT2 'Small Domain'
Homologous superfamily homologous superfamily10 — SIR2/SIRT2 'Small Domain'
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7. Citations (1)