Structure of PDB 4du6 Chain D

Receptor sequence
>4du6D (length=216) Species: 214092 (Yersinia pestis CO92) [Search protein sequence]
SSLSKEAELVHQALLARGLETPLRKPELDAETRKTRIQAHMTEVMHLLNL
DLTDDSLADTPRRIAKMYVDEIFSGLDYENFPKITLIQNKMKVDEMVTVR
DITLTSTCEHHFVTIDGKATVAYIPKDSVIGLSKINRIVQFFAQRPQVQE
RLTQQILLALQTLLGTNNVAVSIDAVHYCVKARGIRDATSATTTTSLGGL
FKSSQNTRQEFLRAVR
3D structure
PDB4du6 Crystal structure of GTP cyclohydrolase I from Yersinia pestis complexed with GTP
ChainD
Resolution2.106 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 D H111 H112 V149 Q150 E151 H178 R184 H110 H111 V148 Q149 E150 H177 R183
BS02 GTP D T86 I131 G132 L133 S134 K135 R138 T85 I130 G131 L132 S133 K134 R137
BS03 CA D H111 H112 C180 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

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Molecular Function
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Cellular Component
External links
PDB RCSB:4du6, PDBe:4du6, PDBj:4du6
PDBsum4du6
PubMed
UniProtQ8ZG15|GCH1_YERPE GTP cyclohydrolase 1 (Gene Name=folE)

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