3GLU: Human SIRT3 with AceCS2 peptide

Crystal Structure of Human SIRT3 with AceCS2 peptide. Determined by X-ray diffraction at 2.5 Å resolution. Released 16 Jun 2009.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,251
Mol. weight: 33.35 kDa
Ligands: ZN
Released: 16 Jun 2009

Explore 3GLU in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3GLU contains 22 α-helices and 13 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 22 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	125-133	9
β-strand	140-144	5	1
α-helix	146-148	3
α-helix	150-152	3
α-helix	154-156	3
α-helix	163-169	7
α-helix	176-180	5
α-helix	182-187	6
α-helix	190-199	10
α-helix	208-218	11
β-strand	222-227	6	1
α-helix	233-236	4
α-helix	241-243	3
β-strand	244-246	3	1
β-strand	249-256	8	2
β-strand	262-264	3	2
α-helix	265-267	3
α-helix	269-273	5
β-strand	279	1	3
α-helix	285	1
β-strand	286	1	3
β-strand	287-291	5	2
α-helix	292-293	2
α-helix	296-299	4
α-helix	300-304	5
α-helix	305-308	4
β-strand	314-318	5	1
β-strand	325	1	4
α-helix	328-332	5
β-strand	340-344	5	1
α-helix	349-353	5
β-strand	359-363	5	1
α-helix	366-376	11
α-helix	380-390	11

Chain B: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	643	1	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
NAD-dependent deacetylase sirtuin-3, mitochondrial	A	protein	285	Homo sapiens	Q9NTG7 (AlphaFold model)
Acetyl-coenzyme A synthetase 2-like, mitochondrial	B	protein	12	Homo sapiens	Q9NUB1 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3GLU_1 NAD-dependent deacetylase sirtuin-3, mitochondrial (chains A)
SNASDKGKLSLQDVAELIRARACQRVVVMVGAGISTPSGIPDFRSPGSGLYSNLQQYDLP
YPEAIFELPFFFHNPKPFFTLAKELYPGNYKPNVTHYFLRLLHDKGLLLRLYTQNIDGLE
RVSGIPASKLVEAHGTFASATCTVCQRPFPGEDIRADVMADRVPRCPVCTGVVKPDIVFF
GEPLPQRFLLHVVDFPMADLLLILGTSLEVEPFASLTEAVRSSVPRLLINRDLVGPLAWH
PRSRDVAQLGDVVHGVESLVELLGWTEEMRDLVQRETGKLDGPDK

Sequence of entity 2 (B), FASTA

>3GLU_2 Acetyl-coenzyme A synthetase 2-like, mitochondrial (chains B)
TRSGKVMRRLLR

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	1

Water and common crystallization additives (SO4) are not listed.

Primary citation

Crystal Structures of Human SIRT3 Displaying Substrate-induced Conformational Changes. Jin, L., Wei, W., Jiang, Y. et al. J Biol Chem (2009) 284:24394-24405. DOI 10.1074/jbc.M109.014928 · PubMed

Other PDB entries of the same protein (UniProt Q9NTG7 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8ANC 1.11 Å, 14-3-3 sigma sirtuin-3 phospho-peptide complex
4BN4 1.3 Å, Structure of human SIRT3 in complex with ADP-ribose
8V5U 1.48 Å, Human SIRT3 bound to p53-AMC peptide and Honokiol
9S27 1.6 Å, Crystal structure of human SIRT3 in complex with the covalent adduct of peptide triazole…
8CCW 1.65 Å, Crystal structure of human Sirt3 in complex with an acetylated HIV1 Tat-46-54 substrate…
4JSR 1.7 Å, Crystal Structure of human SIRT3 with ELT inhibitor 11c…
8V2N 1.74 Å, Human SIRT3 co-crystallized with ligands, including p53-AMC peptide and Carba-NAD
3GLR 1.8 Å, Crystal Structure of human SIRT3 with acetyl-lysine AceCS2 peptide
5D7N 1.83 Å, Crystal structure of human Sirt3 at an improved resolution
5Z94 1.9 Å, Crystal Structure of SIRT3 in complex with H3K4bhb peptide
4BVH 1.9 Å, Crystal structure of human SIRT3 in complex with the inhibitor ex-527 and…
5BWN 1.94 Å, Crystal Structure of SIRT3 with a H3K9 Peptide Containing a Myristoyl Lysine

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