Structure of PDB 1wuq Chain D

Receptor sequence
>1wuqD (length=184) Species: 274 (Thermus thermophilus) [Search protein sequence]
VDLERLQALAAEWLQVIGEDPGREGLLKTPERVAKAWAFLTRGYRQRLEE
VVGGAVFPAEGSEMVVVKGVEFYSMCEHHLLPFFGKVHIGYIPDGKILGL
SKFARIVDMFARRLQVQERLAVQIAEAIQEVLEPQGVGVVVEGVHLCMMM
RGVEKQHSRTVTSAMLGVFRENQKTREEFLSHLR
3D structure
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
ChainD
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 8GT D G131 L132 S133 K134 R137 G99 L100 S101 K102 R105
BS02 ZN D C108 H111 C179 C76 H79 C147
BS03 8GT D H110 H111 V148 Q149 E150 R183 H78 H79 V116 Q117 E118 R151
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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