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Histone lysine desuccinylase SIRT5 in complex with succinyl peptide H2BK120

Analyse Histone lysine desuccinylase SIRT5 in complex with succinyl peptide H2BK120 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6ACO
Type
protein
Length
277 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
NAD-dependent protein deacylase sirtuin-5, mitochondrial; Succinyl peptide H2BK120
EC
3.5.1.-
UniProt
Q9NXA8
Ligands
ZN, CL
Pockets
2 · best druggability 0.39

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ANAD-dependent protein deacylase sirtuin-5, mitochondrial (EC 3.5.1.-)protein27039% helix, 20% strandQ9NXA8
BSuccinyl peptide H2BK120protein70% helix, 43% strand—

Ligands and binding sites

  • ZN · Zinc ion · metal · chains A
  • CL · Chloride ion · ion · chains A
  • GOL · Glycerol · additive · chains B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11190.390.7526empty
2510.280.7515empty

Interfaces

1 interface between chains.

  • A–B · 640 Ų buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (nonstandard).

Compared structures

  • 6ACO · histone lysine desuccinylase Sirt5 in complex with succinyl peptide H2BK120 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9NXA8 · AlphaFold monomer V2.0 prediction for NAD-dependent protein deacylase sirtuin-5… · a predicted model of the same protein · chain A against A, TM-score 0.99

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