Structure of PDB 1wuq Chain A Binding Site BS03

Receptor Information
>1wuq Chain A (length=184) Species: 274 (Thermus thermophilus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VDLERLQALAAEWLQVIGEDPGREGLLKTPERVAKAWAFLTRGYRQRLEE
VVGGAVFPAEGSEMVVVKGVEFYSMCEHHLLPFFGKVHIGYIPDGKILGL
SKFARIVDMFARRLQVQERLAVQIAEAIQEVLEPQGVGVVVEGVHLCMMM
RGVEKQHSRTVTSAMLGVFRENQKTREEFLSHLR
Ligand information
Ligand ID8GT
InChIInChI=1S/C10H16N5O15P3/c11-9-13-6-3(7(18)14-9)12-10(19)15(6)8-5(17)4(16)2(28-8)1-27-32(23,24)30-33(25,26)29-31(20,21)22/h2,4-5,8,16-17H,1H2,(H,12,19)(H,23,24)(H,25,26)(H2,20,21,22)(H3,11,13,14,18)/t2-,4-,5-,8-/m1/s1
InChIKeyJCHLKIQZUXYLPW-UMMCILCDSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C(C1C(C(C(O1)N2C3=C(C(=O)NC(=N3)N)NC2=O)O)O)OP(=O)(O)OP(=O)(O)OP(=O)(O)O
OpenEye OEToolkits 1.5.0C([C@@H]1[C@H]([C@H]([C@@H](O1)N2C3=C(C(=O)NC(=N3)N)NC2=O)O)O)O[P@@](=O)(O)O[P@@](=O)(O)OP(=O)(O)O
CACTVS 3.341NC1=NC2=C(NC(=O)N2[C@@H]3O[C@H](CO[P@](O)(=O)O[P@](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O)C(=O)N1
CACTVS 3.341NC1=NC2=C(NC(=O)N2[CH]3O[CH](CO[P](O)(=O)O[P](O)(=O)O[P](O)(O)=O)[CH](O)[CH]3O)C(=O)N1
ACDLabs 10.04O=P(O)(O)OP(=O)(O)OP(=O)(O)OCC3OC(N2C(=O)NC1=C2N=C(N)NC1=O)C(O)C3O
FormulaC10 H16 N5 O15 P3
Name8-OXO-GUANOSINE-5'-TRIPHOSPHATE
ChEMBLCHEMBL1230627
DrugBank
ZINCZINC000058650735
PDB chain1wuq Chain A Residue 815 [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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PDB1wuq Novel reaction mechanism of GTP cyclohydrolase I. High-resolution X-ray crystallography of Thermus thermophilus HB8 enzyme complexed with a transition state analogue, the 8-oxoguanine derivative
Resolution2.0 Å
Binding residue
(original residue number in PDB)		G131 L132 S133 K134 R137
Binding residue
(residue number reindexed from 1)		G99 L100 S101 K102 R105
Annotation score3
Binding affinityPDBbind-CN: -logKd/Ki=8.27,Ki=0.0054uM
Enzymatic activity
Catalytic site (original residue number in PDB) C108 E109 H110 H111 Q149 H177 C179
Catalytic site (residue number reindexed from 1) C76 E77 H78 H79 Q117 H145 C147
Enzyme Commision number 3.5.4.16: GTP cyclohydrolase I.
Gene Ontology
Molecular Function
GO:0003934 GTP cyclohydrolase I activity
GO:0005525 GTP binding
GO:0008270 zinc ion binding
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0006729 tetrahydrobiopterin biosynthetic process
GO:0006730 one-carbon metabolic process
GO:0046654 tetrahydrofolate biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1wuq, PDBe:1wuq, PDBj:1wuq
PDBsum1wuq
PubMed16169877
UniProtQ5SH52

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