Structure of PDB 1yqn Chain A

Receptor sequence
>1yqnA (length=158) Species: 562 (Escherichia coli) [Search protein sequence]
AEMRIGHGFDVHAFGGEGPIIIGGVRIPYEKGLLAHSDGDVALHALTDAL
LGAAALGDIGKLFPDTDPAFKGADSRELLREAWRRIQAKGYTLGNVDVTI
IAQAPKMLPHIPQMRVFIAEDLGCHMDDVNVKATTTEKLGFTGMGLGIAC
EAVALLIK
3D structure
PDB1yqn A double mutation of Escherichia coli2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase disrupts six hydrogen bonds with, yet fails to prevent binding of, an isoprenoid diphosphate.
ChainA
Resolution3.11 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.6.1.12: 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase.
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 ZN A D8 H10 H42 D10 H12 H44
BS02 CDP A D8 H10 D56 G58 D10 H12 D58 G60
BS03 GPP A F7 G138 F139 F9 G140 F141
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0008270 zinc ion binding
GO:0008685 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity
GO:0016829 lyase activity
GO:0030145 manganese ion binding
GO:0042802 identical protein binding
GO:0046872 metal ion binding
Biological Process
GO:0006744 ubiquinone biosynthetic process
GO:0008299 isoprenoid biosynthetic process
GO:0016114 terpenoid biosynthetic process
GO:0019288 isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway

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Molecular Function
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Biological Process
External links
PDB RCSB:1yqn, PDBe:1yqn, PDBj:1yqn
PDBsum1yqn
PubMed16511114
UniProtP62617|ISPF_ECOLI 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase (Gene Name=ispF)

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