3LLK
Sulfhydryl Oxidase Fragment of Human QSOX1
Summary for 3LLK
| Entry DOI | 10.2210/pdb3llk/pdb |
| Related | 1JR8 1JRA 1OQC 2HJ3 3GWL 3GWN 3LLI |
| Descriptor | Sulfhydryl oxidase 1, FLAVIN-ADENINE DINUCLEOTIDE, CITRATE ANION, ... (4 entities in total) |
| Functional Keywords | sulfhydryl oxidase, disulfide, flavin adenine dinucleotide, alternative splicing, fad, flavoprotein, glycoprotein, golgi apparatus, membrane, oxidoreductase, polymorphism, secreted, transmembrane |
| Biological source | Homo sapiens (human) |
| Cellular location | Isoform 1: Golgi apparatus membrane; Single- pass membrane protein. Isoform 2: Secreted, extracellular space: O00391 |
| Total number of polymer chains | 3 |
| Total formula weight | 91919.99 |
| Authors | |
| Primary citation | Alon, A.,Heckler, E.J.,Thorpe, C.,Fass, D. QSOX contains a pseudo-dimer of functional and degenerate sulfhydryl oxidase domains. Febs Lett., 584:1521-1525, 2010 Cited by PubMed Abstract: Quiescin sulfhydryl oxidase (QSOX) catalyzes formation of disulfide bonds between cysteine residues in substrate proteins. Human QSOX1 is a multi-domain, monomeric enzyme containing a module related to the single-domain sulfhydryl oxidases of the Erv family. A partial QSOX1 crystal structure reveals a single-chain pseudo-dimer mimicking the quaternary structure of Erv enzymes. However, one pseudo-dimer "subunit" has lost its cofactor and catalytic activity. In QSOX evolution, a further concatenation to a member of the protein disulfide isomerase family resulted in an enzyme capable of both disulfide formation and efficient transfer to substrate proteins. PubMed: 20211621DOI: 10.1016/j.febslet.2010.03.001 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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