Structure of PDB 4du6 Chain C

Receptor sequence

>4du6C (length=219) Species: 214092 (Yersinia pestis CO92)

SSLSKEAELVHQALLARGLETPLRKPELDAETRKTRIQAHMTEVMHLLNL
DLTDDSLADTPRRIAKMYVDEIFSGLDYENFPKITLIQNKMKVDEMVTVR
DITLTSTCEHHFVTIDGKATVAYIPKDSVIGLSKINRIVQFFAQRPQVQE
RLTQQILLALQTLLGTNNVAVSIDAVHYCVKARGIRDATSATTTTSLGGL
FKSSQNTRQEFLRAVRHHG

3D structure

• PDB: 4du6 Crystal structure of GTP cyclohydrolase I from Yersinia pestis complexed with GTP
• Chain: C
• Resolution: 2.106 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): C109 E110 H111 H112 Q150 H178 C180
• Catalytic site (residue number reindexed from 1): C108 E109 H110 H111 Q149 H177 C179
• 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	GTP	C	H111 H112 V149 Q150 E151 H178 R184	H110 H111 V148 Q149 E150 H177 R183
BS02	GTP	C	K84 T86 I131 G132 L133 S134 K135 R138	K83 T85 I130 G131 L132 S133 K134 R137
BS03	CA	C	C109 H111 H112 C180	C108 H110 H111 C179

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:4du6, PDBe:4du6, PDBj:4du6
• PDBsum: 4du6
• UniProt: Q8ZG15|GCH1_YERPE GTP cyclohydrolase 1 (Gene Name=folE)