Structure of PDB 4v06 Chain B

Receptor sequence
>4v06B (length=341) Species: 9606 (Homo sapiens) [Search protein sequence]
DVPWFPRKISELDKCSHRVLMYGSELDADHPGFKDNVYRQRRKYFVDVAM
GYKYGQPIPRVEYTEEETKTWGVVFRELSKLYPTHACREYLKNFPLLTKY
CGYREDNVPQLEDVSMFLKERSGFTVRPVAGYLSPRDFLAGLAYRVFHCT
QYIRHGSDPLYTPEPDTCHELLGHVPLLADPKFAQFSQEIGLASLGASDE
DVQKLATCYFFTIEFGLCKQEGQLRAYGAGLLSSIGELKHALSDKACVKA
FDPKTTCLQECLITTFQEAYFVSESFEEAKEKMRDFAKSITRPFSVYFNP
YTQSIEILKDTRSIENVVQDLRSDLNTVCDALNKMNQYLGI
3D structure
PDB4v06 Crystal Structure of Human Tryptophane Hydroxylase 2 (Tph2), Catalytic Domain
ChainB
Resolution2.63 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H318 H323 E363 S382
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 B H318 H323 E363 H169 H174 E214
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:4v06, PDBe:4v06, PDBj:4v06
PDBsum4v06
PubMed
UniProtQ8IWU9|TPH2_HUMAN Tryptophan 5-hydroxylase 2 (Gene Name=TPH2)

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