Structure of PDB 7qri Chain A Binding Site BS01
Receptor Information
>7qri Chain A (length=100) Species:
9606
(Homo sapiens) [
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GPGNKGSSKREAATESGKTAVVFSLKNEVGGLVKALRLFQEKRVNMVHIE
SRKSRRRSSEVEIFVDCECGKTEFNELIQLLKFQTTIVTLNPPENIWTEE
Ligand information
Ligand ID
PHE
InChI
InChI=1S/C9H11NO2/c10-8(9(11)12)6-7-4-2-1-3-5-7/h1-5,8H,6,10H2,(H,11,12)/t8-/m0/s1
InChIKey
COLNVLDHVKWLRT-QMMMGPOBSA-N
SMILES
Software
SMILES
CACTVS 3.341
N[CH](Cc1ccccc1)C(O)=O
CACTVS 3.341
N[C@@H](Cc1ccccc1)C(O)=O
OpenEye OEToolkits 1.5.0
c1ccc(cc1)CC(C(=O)O)N
OpenEye OEToolkits 1.5.0
c1ccc(cc1)C[C@@H](C(=O)O)N
ACDLabs 10.04
O=C(O)C(N)Cc1ccccc1
Formula
C9 H11 N O2
Name
PHENYLALANINE
ChEMBL
CHEMBL301523
DrugBank
DB00120
ZINC
ZINC000000105196
PDB chain
7qri Chain A Residue 201 [
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Receptor-Ligand Complex Structure
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PDB
7qri
Structural characterization of human tryptophan hydroxylase 2 reveals that L-Phe is superior to L-Trp as the regulatory domain ligand.
Resolution
N/A
Binding residue
(original residue number in PDB)
E73 L77 S96
Binding residue
(residue number reindexed from 1)
E28 L32 S51
Annotation score
2
Enzymatic activity
Enzyme Commision number
1.14.16.4
: tryptophan 5-monooxygenase.
Gene Ontology
Molecular Function
GO:0004497
monooxygenase activity
GO:0005506
iron ion binding
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:7qri
,
PDBe:7qri
,
PDBj:7qri
PDBsum
7qri
PubMed
37119821
UniProt
Q8IWU9
|TPH2_HUMAN Tryptophan 5-hydroxylase 2 (Gene Name=TPH2)
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