30KD: Human SIRT2

Crystal structure of human SIRT2 in complex with KMyrMe peptide. Determined by X-ray diffraction at 1.45 Å resolution. Released 30 Sept 2026.

Method
X-ray diffraction
Resolution
1.45 Å
Organisms
Homo sapiens, synthetic construct
Chains
2
Atoms
2,745
Mol. weight
35.65 kDa
Ligands
ZN, BTB, MYR
Released
30 Sept 2026

Explore 30KD in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

30KD contains 17 α-helices and 15 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: 17 helices, 14 β-strands

ElementResiduesLengthSheet
α-helix64-718
β-strand79-8351
α-helix85-873
α-helix89-913
α-helix99-1013
α-helix108-1103
α-helix115-1195
β-strand12012
α-helix121-1266
α-helix129-13810
α-helix147-15711
β-strand161-16661
α-helix172-1754
α-helix180-1823
β-strand183-18531
β-strand188-19583
β-strand203-20533
α-helix206-21510
β-strand22014
β-strand22714
β-strand228-23253
β-strand23512
β-strand23815
α-helix239-2402
α-helix241-25010
β-strand256-26051
α-helix269-2757
β-strand282-28651
β-strand317-32151
α-helix324-33512
α-helix338-35316
Chain C: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand015

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
NAD-dependent protein deacetylase sirtuin-2Aprotein304Homo sapiensQ8IXJ6 (AlphaFold model)
KMyrMe peptideCprotein7synthetic construct
Sequence of entity 1 (A), FASTA
>30KD_1 NAD-dependent protein deacetylase sirtuin-2 (chains A)
GHMERLLDELTLEGVARYMQSERCRRVICLVGAGISTSAGIPDFRSPSTGLYDNLEKYHL
PYPEAIFEISYFKKHPEPFFALAKELYPGQFKPTICHYFMRLLKDKGLLLRCYTQNIDTL
ERIAGLEQEDLVEAHGTFYTSHCVSASCRHEYPLSWMKEKIFSEVTPKCEDCQSLVKPDI
VFFGESLPARFFSCMQSDFLKVDLLLVMGTSLQVQPFASLISKAPLSTPRLLINKEKAGQ
SDPFLGMIMGLGGGMDFDSKKAYRDVAWLGECDQGCLALAELLGWKKELEDLVRREHASI
DAQS
Sequence of entity 2 (C), FASTA
>30KD_2 KMyrMe peptide (chains C)
TARKSTG

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn1
BTB2-[bis-(2-hydroxy-ethyl)-amino]-2-hydroxymethyl-propane-1,3-diolC8 H19 N O51
MYRMyristic acidC14 H28 O21

Primary citation

Enzymatic deacylation of dually modified lysine residues. Friedrich, F., Einsle, O., Jung, M. et al. To be published. DOI 10.1021/acs.biochem.6c00508

Other PDB entries of the same protein (UniProt Q8IXJ6 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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