Structure of PDB 2vnq Chain A

Receptor sequence
>2vnqA (length=176) Species: 511693 (Escherichia coli BL21) [Search protein sequence]
EHVILLNAQGVPTGTLEKYAAHTADTRLHLAFSSWLFNAKGQLLVTRRAL
SKKAWPGVWTNSVCGHPQLGESNEDAVIRRCRYELGVEITPPESIYPDFR
YRATDPSGIVENEVCPVFAARTTSALQINDDEVMDYQWCDLADVLHGIDA
TPWAFSPWMVMQATNREARKRLSAFT
3D structure
PDB2vnq Monoclinic Form of Isopentenyl Diphosphate Isomerase: A Case of Polymorphism in Biomolecular Crystals.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H25 H32 C67 H69 E87 Y104 E114 E116 W161
Catalytic site (residue number reindexed from 1) H22 H29 C64 H66 E84 Y101 E111 E113 W158
Enzyme Commision number 5.3.3.2: isopentenyl-diphosphate Delta-isomerase.
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 MN A H25 H32 H69 E114 E116 H22 H29 H66 E111 E113
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0004452 isopentenyl-diphosphate delta-isomerase activity
GO:0008270 zinc ion binding
GO:0016853 isomerase activity
GO:0046872 metal ion binding
Biological Process
GO:0006974 DNA damage response
GO:0008299 isoprenoid biosynthetic process
GO:0050992 dimethylallyl diphosphate 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:2vnq, PDBe:2vnq, PDBj:2vnq
PDBsum2vnq
PubMed18391416
UniProtQ46822|IDI_ECOLI Isopentenyl-diphosphate Delta-isomerase (Gene Name=idi)

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