Structure of PDB 1wuq Chain B

Receptor sequence

>1wuqB (length=184) Species: 274 (Thermus thermophilus)

VDLERLQALAAEWLQVIGEDPGREGLLKTPERVAKAWAFLTRGYRQRLEE
VVGGAVFPAEGSEMVVVKGVEFYSMCEHHLLPFFGKVHIGYIPDGKILGL
SKFARIVDMFARRLQVQERLAVQIAEAIQEVLEPQGVGVVVEGVHLCMMM
RGVEKQHSRTVTSAMLGVFRENQKTREEFLSHLR

3D structure

• PDB: 1wuq 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
• Chain: B
• Resolution: 2.0 Å

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	B	F89 G131 L132 S133 K134 R137	F57 G99 L100 S101 K102 R105	PDBbind-CN: -logKd/Ki=8.27,Ki=0.0054uM
BS02	ZN	B	C108 H111 C179	C76 H79 C147
BS03	8GT	B	H110 H111 V148 Q149 E150 R183	H78 H79 V116 Q117 E118 R151	PDBbind-CN: -logKd/Ki=8.27,Ki=0.0054uM

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

External links

• PDB: RCSB:1wuq, PDBe:1wuq, PDBj:1wuq
• PDBsum: 1wuq
• PubMed: 16169877
• UniProt: Q5SH52