Structure of PDB 2icj Chain A

Receptor sequence
>2icjA (length=219) Species: 9606 (Homo sapiens) [Search protein sequence]
LDKQQVQLLAEMCILIDENDNKIGAETKKNCHLNENIEKGLLHRAFSVFL
FNTENKLLLQQRSDAKITFPGCFTNTCCSHPLSNPAELEESDALGVRRAA
QRRLKAELGIPLEEVPPEEINYLTRIHYKAQSDGIWGEHEIDYILLVRKN
VTLNPDPNEIKSYCYVSKEELKELLKKAASGEIKITPWFKIIAATFLFKW
WDNLNHLNQFVDHEKIYRM
3D structure
PDB2icj The crystal structure of human isopentenyl diphosphate isomerase at 1.7 A resolution reveals its catalytic mechanism in isoprenoid biosynthesis
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H52 C87 H89 E116 Y137 E147 E149 W197
Catalytic site (residue number reindexed from 1) H43 C78 H80 E107 Y128 E138 E140 W188
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 MG A H41 H52 E147 E149 H32 H43 E138 E140
Gene Ontology
Molecular Function
GO:0004452 isopentenyl-diphosphate delta-isomerase activity
GO:0016853 isomerase activity
GO:0046872 metal ion binding
Biological Process
GO:0006695 cholesterol biosynthetic process
GO:0008299 isoprenoid biosynthetic process
GO:0009240 isopentenyl diphosphate biosynthetic process
GO:0050992 dimethylallyl diphosphate biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005777 peroxisome
GO:0005829 cytosol

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Biological Process
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Cellular Component
External links
PDB RCSB:2icj, PDBe:2icj, PDBj:2icj
PDBsum2icj
PubMed17250851
UniProtQ13907|IDI1_HUMAN Isopentenyl-diphosphate Delta-isomerase 1 (Gene Name=IDI1)

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