6MP5

Crystal structure of native human sulfide:quinone oxidoreductase

External Resource: Annotation

Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Pharos: Disease Associations
Membrane Protein Annotation: mpstruc
Protein Modification Annotation

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF07992	Pyridine nucleotide-disulphide oxidoreductase (Pyr_redox_2)	Pyridine nucleotide-disulphide oxidoreductase	This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Sulfide:quinone oxidoreductase, mitochondrial	oxidoreductase activity, acting on a sulfur group of donors oxidoreductase activity sulfide:quinone oxidoreductase activity catalytic activity oxidoreductase activity, acting on a sulfur group of donors, quinone or similar compound as acceptor glutathione-dependent sulfide quinone oxidoreductase activity FAD binding flavin adenine dinucleotide binding binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding nucleotide binding oxidoreductase activity, acting on a sulfur group of donors oxidoreductase activity sulfide:quinone oxidoreductase activity catalytic activity oxidoreductase activity, acting on a sulfur group of donors, quinone or similar compound as acceptor glutathione-dependent sulfide quinone oxidoreductase activity FAD binding flavin adenine dinucleotide binding binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding nucleotide binding heterocyclic compound binding small molecule binding quinone binding	sulfur compound metabolic process metabolic process cellular process sulfide oxidation, using sulfide:quinone oxidoreductase sulfide oxidation	membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure mitochondrion organelle cytoplasm intracellular membrane-bounded organelle mitochondrial membrane organelle inner membrane membrane mitochondrial inner membrane organelle envelope mitochondrial envelope membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure mitochondrion organelle cytoplasm intracellular membrane-bounded organelle mitochondrial membrane organelle inner membrane membrane mitochondrial inner membrane organelle envelope mitochondrial envelope organelle membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR015904	Sulphide quinone-reductase	Family
A, B, C, D	IPR023753	FAD/NAD(P)-binding domain	Domain
A, B, C, D	IPR036188	FAD/NAD(P)-binding domain superfamily	Homologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C, D	Pharos: Q9Y6N5	adrenal cortex carcinoma juvenile idiopathic arthritis malignant colon neoplasm medulloblastoma pilocytic astrocytoma psoriasis ethylmalonic encephalopathy large cell medulloblastoma malignant glioma osteosarcoma pituitary cancer rheumatoid arthritis glioblastoma lung cancer malignant mesothelioma adrenal cortex carcinoma juvenile idiopathic arthritis malignant colon neoplasm medulloblastoma pilocytic astrocytoma psoriasis ethylmalonic encephalopathy large cell medulloblastoma malignant glioma osteosarcoma pituitary cancer rheumatoid arthritis glioblastoma lung cancer malignant mesothelioma ovarian cancer plasma cell myeloma subependymal giant cell astrocytoma

Membrane Protein Annotation: mpstruc mpstruc Database Homepage

Chains	Resource Link	Group	Subgroup	Protein
A, B, C, D	mpstruc	MONOTOPIC MEMBRANE PROTEINS	Oxidoreductases (Monotopic)	Sulfide:quinone oxidoreductase, selenomethionine-substituted

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A, B, C, D	CSS	Parent Component: CYS RESID: AA0269 PSI-MOD : L-cysteine persulfide MOD:00274

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.