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Structure of PDB 5mms Chain E

Receptor sequence >5mmsE (length=349) Species: 9606 (Homo sapiens) [Search protein sequence] IRPDALSRCTWQLGRPASESPHHHTAPAKSPKILPDILKKIGDTPMVRIN KIGKKFGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTII EPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPT NARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQQ CDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSILAEPEEL NTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGG SAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGFL

3D structure PDB 5mms A Clinically Relevant Variant of the Human Hydrogen Sulfide-Synthesizing Enzyme Cystathionine beta-Synthase: Increased CO Reactivity as a Novel Molecular Mechanism of Pathogenicity? Chain E Resolution 2.8 Å 3D structure Catalytic site residues are labeled in the structure [Spin on] [Spin off] [Reset orientation] [High quality] [Low quality] [White background] [Black background] [Download] [Download structure with residue number starting from 1]

Enzymatic activity Catalytic site (original residue number in PDB) K119 S147 D281 S285 L287 S349 P375 Catalytic site (residue number reindexed from 1) K76 S104 D238 S242 L244 S301 P327 Enzyme Commision number 4.2.1.22: cystathionine beta-synthase.

Interaction with ligand Site # Ligand Ligand chain Binding residues on receptor (original residue number in PDB) Binding residues on receptor (residue number reindexed from 1) Binding affinity BS01 HEM E S50 R51 C52 T53 W54 R58 E62 S63 P64 H65 A226 P229 L230 Y233 R266 S7 R8 C9 T10 W11 R15 E19 S20 P21 H22 A183 P186 L187 Y190 R223 BS02 PLP E K119 N149 G256 T257 G258 T260 G305 S349 P375 D376 K76 N106 G213 T214 G215 T217 G257 S301 P327 D328

Gene Ontology Molecular Function GO:0004122 cystathionine beta-synthase activity

	Biological Process
GO:0006535	cysteine biosynthetic process from serine
GO:0019343	cysteine biosynthetic process via cystathionine

	Cellular Component
GO:0005737	cytoplasm

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