Sandbox Reserved 1126
From Proteopedia
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== Structure == | == Structure == | ||
- | A CBS monomer is natively a 63 kDa protein made of 551 amino-acids and each of them binds two cofactors (the iron heme and the pyridoxal phosphate), as well as two substrates (homocysteine and serine). Hence, the CBS contains (from N-terminal to C-terminal) a heme binding site | + | A CBS monomer is natively a 63 kDa protein made of 551 amino-acids and each of them binds two cofactors (the iron heme and the pyridoxal phosphate), as well as two substrates (homocysteine and serine). Hence, the CBS contains (from N-terminal to C-terminal): |
+ | - a heme binding site located in a hydrophobic pocket (residues 50-67) | ||
+ | - a pyridoxal phosphate (covalently linked to Lysine 119 amino group) situated in a highly conserved central catalytic domain (residues 70-382) | ||
+ | - a C-terminal regulatory domain called Bateman module composed of two CBS domains (CBS 1 and CBS 2) | ||
IMAGE ALICE | IMAGE ALICE | ||
Revision as of 12:18, 29 January 2016
This Sandbox is Reserved from 15/12/2015, through 15/06/2016 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1120 through Sandbox Reserved 1159. |
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Human cystathionine β-synthase (hCBS)
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