Structure of PDB 2toh Chain A Binding Site BS02

Receptor Information
>2toh Chain A (length=336) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
REDKVPWFPRKVSELDKCHHLVTPDLDLDHPGFSDQVYRQRRKLIAEIAF
QYKHGEPIPHVEYTAEEIATWKEVYVTLKGLYATHACREHLEGFQLLERY
CGYREDSIPQLEDVSRFLKERTGFQLRPVAGLLSARDYLASLAFRVFQCT
QYIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGASDE
EIEKLSTVYWFTVEFGLCKQNGELKAYGAGLLSSYGELLHSLSEEPEVRA
FDPDTAAVQPYQDQTYQPVYFVSESFNDAKDKLRNYASRIQRPFSVKFDP
YTLAIDVLDSPHTIQRSLEGVQDELHTLAHALSAIS
Ligand information
Ligand IDHBI
InChIInChI=1S/C9H13N5O3/c1-3(15)6(16)4-2-11-7-5(12-4)8(17)14-9(10)13-7/h3,6,15-16H,2H2,1H3,(H4,10,11,13,14,17)/t3-,6-/m0/s1
InChIKeyFEMXZDUTFRTWPE-DZSWIPIPSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CC(C(C1=NC2=C(NC1)N=C(NC2=O)N)O)O
OpenEye OEToolkits 1.5.0C[C@@H]([C@@H](C1=NC2=C(NC1)N=C(NC2=O)N)O)O
CACTVS 3.341C[C@H](O)[C@H](O)C1=NC2=C(NC1)N=C(N)NC2=O
ACDLabs 10.04O=C1NC(=NC=2NCC(=NC1=2)C(O)C(O)C)N
CACTVS 3.341C[CH](O)[CH](O)C1=NC2=C(NC1)N=C(N)NC2=O
FormulaC9 H13 N5 O3
Name7,8-DIHYDROBIOPTERIN
ChEMBL
DrugBankDB04400
ZINCZINC000018181336
PDB chain2toh Chain A Residue 500 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB2toh Crystal structure of tyrosine hydroxylase with bound cofactor analogue and iron at 2.3 A resolution: self-hydroxylation of Phe300 and the pterin-binding site.
Resolution2.3 Å
Binding residue
(original residue number in PDB)		V291 L294 L295 X300 P327 E332 Y371
Binding residue
(residue number reindexed from 1)		V129 L132 L133 X138 P165 E170 Y209
Annotation score2
Binding affinityMOAD: Ki=70uM
PDBbind-CN: -logKd/Ki=4.15,Ki=70uM
Enzymatic activity
Catalytic site (original residue number in PDB) H331 H336 E376 S395
Catalytic site (residue number reindexed from 1) H169 H174 E214 S233
Enzyme Commision number 1.14.16.2: tyrosine 3-monooxygenase.
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:2toh, PDBe:2toh, PDBj:2toh
PDBsum2toh
PubMed9753429
UniProtP04177|TY3H_RAT Tyrosine 3-monooxygenase (Gene Name=Th)

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