1mlw | pdb_00001mlw

Crystal structure of human tryptophan hydroxylase with bound 7,8-dihydro-L-biopterin cofactor and Fe(III)

spinqualitylabelsall models 1mlw, resolution 1.71Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1mlw is a 1 chain structure with sequence from Human. The January 2005 RCSB PDB Molecule of the Month feature on Phenylalanine Hydroxylase by Shuchismita Dutta and David S. Goodsell is 10.2210/rcsb_pdb/mom_2005_1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FE, HBI Gene: TPH (HUMAN) Activity: Tryptophan 5-monooxygenase, with EC number 1.14.16.4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Tryptophan hydroxylase oxidizes L-tryptophan to 5-hydroxy-L-tryptophan in the rate-determining step of serotonin biosynthesis. We have determined the X-ray crystal structure (1.7 A) of a truncated functional form of human tryptophan hydroxylase with the bound cofactor analogue 7,8-dihydro-L-biopterin, providing the first atomic-resolution information for the catalytic domain of this important enzyme. Comparison of the three-dimensional structures of all three members of the aromatic amino acid hydroxylase family--tyrosine hydroxylase, phenylalanine hydroxylase, and tryptophan hydroxylase--reveals important differences at the active sites. Three-dimensional structure of human tryptophan hydroxylase and its implications for the biosynthesis of the neurotransmitters serotonin and melatonin.,Wang L, Erlandsen H, Haavik J, Knappskog PM, Stevens RC Biochemistry. 2002 Oct 22;41(42):12569-74. PMID:12379098 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Tryptophan hydroxylase Tryptophan hydroxylase 1 with bound tryptophan

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