Structure of PDB 2i6k Chain A

Receptor sequence

>2i6kA (length=224) Species: 9606 (Homo sapiens)

INTNHLDKQQVQLLAEMCILIDENDNKIGAETKKNCHLNENIEKGLLHRA
FSVFLFNTENKLLLQQRSDAKITFPGCFTNTCCSHPLSNPAELEESDALG
VRRAAQRRLKAELGIPLEEVPPEEINYLTRIHYKAQSDGIWGEHEIDYIL
LVRMNVTLNPDPNEIKSYCYVSKEELKELLKKAASGEIKITPWFKIIAAT
FLFKWWDNLNHLNQFVDHEKIYRM

3D structure

• PDB: 2i6k Crystal structures of human IPP isomerase: new insights into the catalytic mechanism
• Chain: A
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H51 C86 H88 E115 Y136 E146 E148 W196
• Catalytic site (residue number reindexed from 1): H48 C83 H85 E112 Y133 E143 E145 W193
• 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	H40 H51 H88 E146 E148	H37 H48 H85 E143 E145
BS02	MG	A	C86 E115	C83 E112
BS03	MG	A	E97 S99	E94 S96
BS04	EA2	A	K36 R70 C86 S87 H88 R111 E148	K33 R67 C83 S84 H85 R108 E145

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

External links

• PDB: RCSB:2i6k, PDBe:2i6k, PDBj:2i6k
• PDBsum: 2i6k
• PubMed: 17137593
• UniProt: Q13907|IDI1_HUMAN Isopentenyl-diphosphate Delta-isomerase 1 (Gene Name=IDI1)