Structure of PDB 2i6k Chain B

Receptor sequence

>2i6kB (length=220) Species: 9606 (Homo sapiens)

HLDKQQVQLLAEMCILIDENDNKIGAETKKNCHLNENIEKGLLHRAFSVF
LFNTENKLLLQQRSDAKITFPGCFTNTCCSHPLSNPAELEESDALGVRRA
AQRRLKAELGIPLEEVPPEEINYLTRIHYKAQSDGIWGEHEIDYILLVRM
NVTLNPDPNEIKSYCYVSKEELKELLKKAASGEIKITPWFKIIAATFLFK
WWDNLNHLNQFVDHEKIYRM

3D structure

• PDB: 2i6k Crystal structures of human IPP isomerase: new insights into the catalytic mechanism
• Chain: B
• 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): H44 C79 H81 E108 Y129 E139 E141 W189
• 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	B	H40 H51 H88 E146 E148	H33 H44 H81 E139 E141
BS02	MG	B	C86 E115	C79 E108
BS03	MG	B	E97 S99	E90 S92
BS04	EA2	B	K36 R70 K74 C86 S87 H88 R111 E115 E148	K29 R63 K67 C79 S80 H81 R104 E108 E141

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)