8Z58: Human N141V-SIRT5

Crystal structure of human N141V-SIRT5 in complex with succinylated Prx1 fragment. Determined by X-ray diffraction at 2.4 Å resolution. Released 9 Oct 2024.

Method
X-ray diffraction
Resolution
2.4 Å
Organism
Homo sapiens
Chains
2
Atoms
2,113
Mol. weight
31.35 kDa
Ligands
ZN
Released
9 Oct 2024

Explore 8Z58 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8Z58 contains 18 α-helices and 16 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: 18 helices, 15 β-strands

ElementResiduesLengthSheet
β-strand3711
α-helix40-4910
β-strand52-5761
α-helix59-635
β-strand7712
β-strand8012
α-helix82-854
α-helix88-936
α-helix95-10814
α-helix116-13015
β-strand134-13961
α-helix145-1495
β-strand154-15631
β-strand159-16683
β-strand172-17433
α-helix182-1843
α-helix194-1963
α-helix201-2033
β-strand20614
α-helix2141
β-strand21514
β-strand216-22053
α-helix221-2222
α-helix2251
β-strand22615
α-helix227-2282
α-helix229-24113
β-strand244-24851
α-helix257-2593
α-helix260-2656
β-strand271-27551
β-strand287-29041
α-helix293-3008
Chain B: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand12115

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
NAD-dependent protein deacylase sirtuin-5, mitochondrialAprotein274Homo sapiensQ9NXA8 (AlphaFold model)
Peroxiredoxin-1 fragmentBprotein9Homo sapiensQ06830 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>8Z58_1 NAD-dependent protein deacylase sirtuin-5, mitochondrial (chains A)
MHHHHHHPSSSMADFRKFFAKAKHIVIISGAGVSAESGVPTFRGAGGYWRKWQAQDLATP
LAFAHNPSRVWEFYHYRREVMGSKEPNAGHRAIAECETRLGKQGRRVVVITQVIDELHRK
AGTKNLLEIHGSLFKTRCTSCGVVAENYKSPICPALSGKGAPEPGTQDASIPVEKLPRCE
EAGCGGLLRPHVVWFGENLDPAILEEVDRELAHCDLCLVVGTSSVVYPAAMFAPQVAARG
VPVAEFNTETTPATNRFRFHFQGPCGTTLPEALA
Sequence of entity 2 (B), FASTA
>8Z58_2 Peroxiredoxin-1 fragment (chains B)
SKEYFSXQK

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn1

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

Primary citation

SIRT5 mutants reveal the role of conserved asparagine and glutamine residues in the NAD + -binding pocket. Yokoyama, T., Takayama, Y., Mizuguchi, M. et al. FEBS Lett (2024) 598:2269-2280. DOI 10.1002/1873-3468.14961 · PubMed

Other PDB entries of the same protein (UniProt Q9NXA8 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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