Structure of PDB 1wur Chain C

Receptor sequence
>1wurC (length=185) Species: 274 (Thermus thermophilus) [Search protein sequence]
EVDLERLQALAAEWLQVIGEDPGREGLLKTPERVAKAWAFLTRGYRQRLE
EVVGGAVFPAEGSEMVVVKGVEFYSMCEHHLLPFFGKVHIGYIPDGKILG
LSKFARIVDMFARRLQVQERLAVQIAEAIQEVLEPQGVGVVVEGVHLCMM
MRGVEKQHSRTVTSAMLGVFRENQKTREEFLSHLR
3D structure
PDB1wur 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
ChainC
Resolution1.82 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) C77 E78 H79 H80 Q118 H146 C148
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 ZN C C108 H111 C179 C77 H80 C148
BS02 8DG C G131 L132 S133 K134 R137 G100 L101 S102 K103 R106
BS03 8DG C H110 H111 V148 Q149 E150 C179 R183 H79 H80 V117 Q118 E119 C148 R152
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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Cellular Component
External links
PDB RCSB:1wur, PDBe:1wur, PDBj:1wur
PDBsum1wur
PubMed16169877
UniProtQ5SH52

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