AlphaFold predicted structure
COX5B · P10606
Mean pLDDT
84.6/ 100
Confident
129 residues
Confidence breakdown
- Very high(≥ 90)67%
- Confident(70–90)6%
- Low(50–70)24%
- Very low(< 50)3%
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AlphaFold (Jumper et al., 2021) · CC BY 4.0
COX5B
Chr 2q11.2cytochrome c oxidase subunit 5B
- MANE:
- ENST00000258424.3
Annotations refreshed 9 hours ago.
Predicted protein structure
Clinical relevance (Genomics England PanelApp)
Moderate Evidence (Amber)
Mitochondrial disorder with complex IV deficiency
UnknownPossible mitochondrial disorder - nuclear genes
UnknownLikely inborn error of metabolism
UnknownMitochondrial disorders
Disease associations (Open Targets)
neurodegenerative disease
0.44autoimmune disorder of central nervous system
0.29poisoning
0.23thyroid gland disorder
0.12Hashimoto thyroiditis
0.09breast cancer
0.08breast carcinoma
0.08hepatocellular carcinoma
0.08retinitis pigmentosa
0.08Cone rod dystrophy
0.07
Score is the Open Targets composite evidence score (0-1). Higher = stronger gene-disease association.
Protein function (UniProt)
Cytochrome c oxidase subunit 5B, mitochondrial
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