Q9NXA8: NAD-dependent protein deacylase sirtuin-5, mitochondrial (SIRT5)

NAD-dependent protein deacylase sirtuin-5, mitochondrial (SIRT5) is a 310-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9NXA8.

Gene
SIRT5
Organism
Homo sapiens
Length
310 residues
Mean pLDDT
89.8
Model
AF-Q9NXA8-F1 v6
Model created
1 Aug 2025
PDB structures
26

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Model confidence (pLDDT)

The mean pLDDT of this model is 89.8 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate84%
70 to 90Confident: backbone generally right3%
50 to 70Low: treat with caution3%
Below 50Very low: often disordered regions10%

What pLDDT means and how to read it

Function

NAD-dependent lysine demalonylase, desuccinylase and deglutarylase that specifically removes malonyl, succinyl and glutaryl groups on target proteins (PubMed:21908771, PubMed:22076378, PubMed:24703693, PubMed:29180469). Activates CPS1 and contributes to the regulation of blood ammonia levels during prolonged fasting: acts by mediating desuccinylation and deglutarylation of CPS1, thereby increasing CPS1 activity in response to elevated NAD levels during fasting (PubMed:22076378, PubMed:24703693). Activates SOD1 by mediating its desuccinylation, leading to reduced reactive oxygen species (PubMed:24140062). Activates SHMT2 by mediating its desuccinylation (PubMed:29180469). Modulates…

Subunit structure

Interacts with CPS1 (By similarity). Interacts with PCCA (PubMed:23438705). Monomer (PubMed:17355872). Homodimer (PubMed:17355872). Forms homodimers upon suramin binding (PubMed:17355872)

Subcellular location

Mitochondrion matrix, Mitochondrion intermembrane space, Cytoplasm, cytosol, Nucleus, Cytoplasm, Mitochondrion

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
6EQSX-ray1.32 ÅA/B/C/D=34-302
6LJKX-ray1.39 ÅA=34-302
8Z54X-ray1.45 ÅA=36-302
3RIYX-ray1.55 ÅA/B=34-302
5BWLX-ray1.55 ÅA=33-302
7X3PX-ray1.56 ÅA=34-310
4F56X-ray1.7 ÅA/B=34-302
6ACOX-ray1.71 ÅA=34-302
6LJMX-ray1.78 ÅA=34-302
6LJNX-ray1.8 ÅA=34-302
8Z56X-ray1.81 ÅA=36-302
8Z55X-ray1.83 ÅA=36-302
2B4YX-ray1.9 ÅA/B/C/D=34-302
6ACLX-ray1.92 ÅA=36-302
4G1CX-ray1.94 ÅA/B=36-302
8Z57X-ray1.96 ÅA=36-302
6ACEX-ray1.98 ÅA=36-302
3RIGX-ray2.0 ÅA/B=34-302
4F4UX-ray2.0 ÅA/B=34-302
2NYRX-ray2.06 ÅA/B=34-302

Showing 20 of 26 experimental structures (best resolution first).

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