Structure of PDB 1mlw Chain A

Receptor sequence
>1mlwA (length=290) Species: 9606 (Homo sapiens) [Search protein sequence]
SVPWFPKKISDLDHCANRVLMYGSELDADHPGFKDNVYRKRRKYFADLAM
NYKHGDPIPKVEFTEEEIKTWGTVFRELNKLYPTHACREYLKNLPLLSKY
CGYREDNIPQLEDVSNFLKERTGFSIRPVAGYLSPRDFLSGLAFRVFHCT
QYVRHSSDPFYTPEPDTCHELLGHVPLLAEPSFAQFSQEIGLASLGASEE
AVQKLATCYFFTVEFGLCKQDGQLRVFGAGLLSSISELKHALSGHAKVKP
FDPKITCKQECLITTFQDVYFVSESFEDAKEKMREFTKTI
3D structure
PDB1mlw Three-dimensional structure of human tryptophan hydroxylase and its implications for the biosynthesis of the neurotransmitters serotonin and melatonin
ChainA
Resolution1.71 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H272 H277 E317 S336
Catalytic site (residue number reindexed from 1) H169 H174 E214 S233
Enzyme Commision number 1.14.16.4: tryptophan 5-monooxygenase.
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 FE A H272 H277 E317 H169 H174 E214
BS02 HBI A Y235 L236 P238 F241 Y312 Y132 L133 P135 F138 Y209
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0016714 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced pteridine as one donor, and incorporation of one atom of oxygen
Biological Process
GO:0009072 aromatic amino acid metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1mlw, PDBe:1mlw, PDBj:1mlw
PDBsum1mlw
PubMed12379098
UniProtP17752|TPH1_HUMAN Tryptophan 5-hydroxylase 1 (Gene Name=TPH1)

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