O43464: Serine protease HTRA2, mitochondrial (HTRA2)

Serine protease HTRA2, mitochondrial (HTRA2) is a 458-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O43464.

Gene
HTRA2
Organism
Homo sapiens
Length
458 residues
Mean pLDDT
74.4
Model
AF-O43464-F1 v6
Model created
1 Aug 2025
PDB structures
13

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Model confidence (pLDDT)

The mean pLDDT of this model is 74.4 (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 accurate52%
70 to 90Confident: backbone generally right12%
50 to 70Low: treat with caution7%
Below 50Very low: often disordered regions30%

What pLDDT means and how to read it

Function

Serine protease that shows proteolytic activity against a non-specific substrate beta-casein (PubMed:10873535). Promotes apoptosis by either relieving the inhibition of BIRC proteins on caspases, leading to an increase in caspase activity; or by a BIRC inhibition-independent, caspase-independent and serine protease activity-dependent mechanism (PubMed:15200957). Cleaves BIRC6 and relieves its inhibition on CASP3, CASP7 and CASP9, but it is also prone to inhibition by BIRC6 (PubMed:36758104, PubMed:36758105). Cleaves THAP5 and promotes its degradation during apoptosis (PubMed:19502560)

Subunit structure

Homotrimer (PubMed:36758104, PubMed:36758105). Interacts with MXI2. Interacts with THAP5 under apoptotic conditions. The mature protein, but not the precursor, binds to BIRC2/c-IAP1, BIRC3/c-IAP2 and XIAP/BIRC4. Interacts with AREL1 (via HECT domain); in the cytoplasm following induction of apoptosis (PubMed:23479728)

Subcellular location

Mitochondrion intermembrane space, Mitochondrion membrane, Endoplasmic reticulum

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5M3NX-ray1.65 ÅA=134-458
5TO1X-ray1.69 ÅA=134-458
5M3OX-ray1.7 ÅA=134-458
5TNYX-ray1.7 ÅA=134-458
5TNZX-ray1.75 ÅA=134-458
5TO0X-ray1.9 ÅA=134-458
5FHTX-ray1.95 ÅA=134-458
1LCYX-ray2.0 ÅA=134-458
5WYNX-ray2.05 ÅA=134-458
2PZDX-ray2.75 ÅA/B=359-458
8E2KEM3.21 ÅX/Y/Z=134-458
7VGEX-ray4.0 ÅA/B/C=140-342, D/F=140-341, E=140-340
8AUKEM6.2 ÅC/D/E=134-458

More AlphaFold highlights

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