AlphaFold predicted structure
MT-CO2 · P00403
Mean pLDDT
94.8/ 100
Very high
227 residues
Confidence breakdown
- Very high(≥ 90)91%
- Confident(70–90)6%
- Low(50–70)1%
- Very low(< 50)1%
Open interactive 3D viewer
AlphaFold (Jumper et al., 2021) · CC BY 4.0
MT-CO2
Chr mitochondriamitochondrially encoded cytochrome c oxidase II
- Aliases:
- COX2, CO2
Annotations refreshed 10 hours ago.
Predicted protein structure
Clinical relevance (Genomics England PanelApp)
Diagnostic Grade (Green)
Acute rhabdomyolysis
MITOCHONDRIALLikely inborn error of metabolism
MITOCHONDRIALMitochondrial disorders
MITOCHONDRIALRhabdomyolysis and metabolic muscle disorders
MITOCHONDRIALUndiagnosed metabolic disorders
MITOCHONDRIALChildhood onset dystonia, chorea or related movement disorder
MITOCHONDRIAL
Disease associations (Open Targets)
mitochondrial disease
0.71Isolated cytochrome C oxidase deficiency
0.70MELAS syndrome
0.57leigh syndrome due to mitochondrial complex iv deficiency
0.54MERRF
0.52MERRF syndrome
0.52mitochondrial non-syndromic sensorineural hearing loss
0.49Mitochondrial myopathy
0.49inborn mitochondrial myopathy
0.49Abnormal mitral valve physiology
0.45
Score is the Open Targets composite evidence score (0-1). Higher = stronger gene-disease association.
Protein function (UniProt)
Cytochrome c oxidase subunit 2
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix
Diseases associated with MT-CO2
Curated MONDO disease pages that list MT-CO2 among their top associated genes.