Structure of PDB 4du6 Chain E

Receptor sequence
>4du6E (length=214) Species: 214092 (Yersinia pestis CO92) [Search protein sequence]
SSLSKEAELVHQALLARGLETPPELDAETRKTRIQAHMTEVMHLLNLDLT
DDSLADTPRRIAKMYVDEIFSGLDYENFPKITLIQNKMKVDEMVTVRDIT
LTSTCEHHFVTIDGKATVAYIPKDSVIGLSKINRIVQFFAQRPQVQERLT
QQILLALQTLLGTNNVAVSIDAVHYCVKARGIRDATSATTTTSLGGLFKS
SQNTRQEFLRAVRH
3D structure
PDB4du6 Crystal structure of GTP cyclohydrolase I from Yersinia pestis complexed with GTP
ChainE
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) C105 E106 H107 H108 Q146 H174 C176
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 E H111 H112 V149 Q150 E151 H178 C180 R184 H107 H108 V145 Q146 E147 H174 C176 R180
BS02 GTP E T86 I131 G132 L133 S134 K135 R138 T82 I127 G128 L129 S130 K131 R134
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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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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