Structure of PDB 4du6 Chain D Binding Site BS03

Receptor Information
>4du6 Chain D (length=216) Species: 214092 (Yersinia pestis CO92) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SSLSKEAELVHQALLARGLETPLRKPELDAETRKTRIQAHMTEVMHLLNL
DLTDDSLADTPRRIAKMYVDEIFSGLDYENFPKITLIQNKMKVDEMVTVR
DITLTSTCEHHFVTIDGKATVAYIPKDSVIGLSKINRIVQFFAQRPQVQE
RLTQQILLALQTLLGTNNVAVSIDAVHYCVKARGIRDATSATTTTSLGGL
FKSSQNTRQEFLRAVR
Ligand information
Ligand IDCA
InChIInChI=1S/Ca/q+2
InChIKeyBHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Ca+2]
FormulaCa
NameCALCIUM ION
ChEMBL
DrugBankDB14577
ZINC
PDB chain4du6 Chain D Residue 304 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4du6 Crystal structure of GTP cyclohydrolase I from Yersinia pestis complexed with GTP
Resolution2.106 Å
Binding residue
(original residue number in PDB)		H111 H112 C180
Binding residue
(residue number reindexed from 1)		H110 H111 C179
Annotation score1
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.
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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Biological Process
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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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