1MLW
Crystal structure of human tryptophan hydroxylase with bound 7,8-dihydro-L-biopterin cofactor and Fe(III)
Summary for 1MLW
| Entry DOI | 10.2210/pdb1mlw/pdb |
| Descriptor | Tryptophan 5-monooxygenase, FE (III) ION, 7,8-DIHYDROBIOPTERIN, ... (4 entities in total) |
| Functional Keywords | aromatic amino acid hydroxylase catalytic domain fold, oxidoreductase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 34936.60 |
| Authors | Wang, L.,Erlandsen, H.,Haavik, J.,Knappskog, P.M.,Stevens, R.C. (deposition date: 2002-08-31, release date: 2002-12-18, Last modification date: 2024-02-14) |
| Primary citation | Wang, L.,Erlandsen, H.,Haavik, J.,Knappskog, P.M.,Stevens, R.C. Three-dimensional structure of human tryptophan hydroxylase and its implications for the biosynthesis of the neurotransmitters serotonin and melatonin Biochemistry, 41:12569-12574, 2002 Cited by PubMed Abstract: 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. PubMed: 12379098DOI: 10.1021/bi026561f PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.71 Å) |
Structure validation
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