Structure of PDB 1wpl Chain A Binding Site BS01

Receptor Information
>1wpl Chain A (length=194) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
RPRSEEDNELNLPNLAAAYSSILRSLGEDPQRQGLLKTPWRAATAMQFFT
KGYQETISDVLNDAIFDEDHDEMVIVKDIDMFSMCEHHLVPFVGRVHIGY
LPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALQPAGVGVVI
EATHMCMVMRGVQKMNSKTVTSTMLGVFREDPKTREEFLTLIRS
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain1wpl Chain A Residue 1110 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1wpl Structural basis of biopterin-induced inhibition of GTP cyclohydrolase I by GFRP, its feedback regulatory protein
Resolution2.8 Å
Binding residue
(original residue number in PDB)		C132 H135 C203
Binding residue
(residue number reindexed from 1)		C85 H88 C156
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) C132 E133 H134 H135 Q173 H201 C203
Catalytic site (residue number reindexed from 1) C85 E86 H87 H88 Q126 H154 C156
Enzyme Commision number 3.5.4.16: GTP cyclohydrolase I.
Gene Ontology
Molecular Function
GO:0003924 GTPase activity
GO:0003934 GTP cyclohydrolase I activity
GO:0005509 calcium ion binding
GO:0005515 protein binding
GO:0005525 GTP binding
GO:0008270 zinc ion binding
GO:0016787 hydrolase activity
GO:0030742 GTP-dependent protein binding
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:0044877 protein-containing complex binding
GO:0046872 metal ion binding
GO:0051019 mitogen-activated protein kinase binding
Biological Process
GO:0006729 tetrahydrobiopterin biosynthetic process
GO:0008217 regulation of blood pressure
GO:0010460 positive regulation of heart rate
GO:0010667 negative regulation of cardiac muscle cell apoptotic process
GO:0014916 regulation of lung blood pressure
GO:0032212 positive regulation of telomere maintenance via telomerase
GO:0032496 response to lipopolysaccharide
GO:0034341 response to type II interferon
GO:0034612 response to tumor necrosis factor
GO:0042311 vasodilation
GO:0042416 dopamine biosynthetic process
GO:0042559 pteridine-containing compound biosynthetic process
GO:0043525 positive regulation of neuron apoptotic process
GO:0045776 negative regulation of blood pressure
GO:0046654 tetrahydrofolate biosynthetic process
GO:0048265 response to pain
GO:0050884 neuromuscular process controlling posture
GO:0051000 positive regulation of nitric-oxide synthase activity
GO:0051066 dihydrobiopterin metabolic process
GO:0065003 protein-containing complex assembly
GO:2000121 regulation of removal of superoxide radicals
GO:2000773 negative regulation of cellular senescence
Cellular Component
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005829 cytosol
GO:0031410 cytoplasmic vesicle
GO:0031965 nuclear membrane
GO:0032991 protein-containing complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1wpl, PDBe:1wpl, PDBj:1wpl
PDBsum1wpl
PubMed15448133
UniProtP22288|GCH1_RAT GTP cyclohydrolase 1 (Gene Name=Gch1)

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