Q96HY7: 2-oxoadipate dehydrogenase complex component E1 (DHTKD1)

2-oxoadipate dehydrogenase complex component E1 (DHTKD1) is a 919-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q96HY7.

Gene
DHTKD1
Organism
Homo sapiens
Length
919 residues
Mean pLDDT
95.1
Model
AF-Q96HY7-F1 v6
Model created
1 Aug 2025
PDB structures
8

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Model confidence (pLDDT)

The mean pLDDT of this model is 95.1 (very high 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 accurate92%
70 to 90Confident: backbone generally right4%
50 to 70Low: treat with caution1%
Below 50Very low: often disordered regions3%

What pLDDT means and how to read it

Function

2-oxoadipate dehydrogenase (E1a) component of the 2-oxoadipate dehydrogenase complex (OADHC) (PubMed:29191460, PubMed:29752936, PubMed:32303640, PubMed:32633484, PubMed:32695416). Participates in the first step, rate limiting for the overall conversion of 2-oxoadipate (alpha-ketoadipate) to glutaryl-CoA and CO(2) catalyzed by the whole OADHC (PubMed:29191460, PubMed:32695416). Catalyzes the irreversible decarboxylation of 2-oxoadipate via the thiamine diphosphate (ThDP) cofactor and subsequent transfer of the decarboxylated acyl intermediate on an oxidized dihydrolipoyl group that is covalently amidated to the E2 enzyme (dihydrolipoyllysine-residue succinyltransferase or DLST) (Probable)…

Subunit structure

The 2-oxoadipate dehydrogenase complex is composed of OADH (2-oxoadipate dehydrogenase; E1a), DLST (dihydrolipoamide succinyltransferase; E2) and DLD (dihydrolipoamide dehydrogenase; E3). E1a functional unit is a dimer. Interacts with DLST (PubMed:32695416)

Subcellular location

Mitochondrion

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5RW1X-ray1.52 ÅA/B=45-919
5RVWX-ray1.61 ÅA/B=45-919
5RVYX-ray1.61 ÅA/B=45-919
5RVXX-ray1.66 ÅA/B=45-919
5RW0X-ray1.67 ÅA/B=45-919
6SY1X-ray1.87 ÅA/B=45-919
5RVZX-ray1.98 ÅA/B=45-919
6U3JX-ray2.25 ÅA/B=25-919

More AlphaFold highlights

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