2icj

The crystal structure of human isopentenyl diphophate isomeraseThe crystal structure of human isopentenyl diphophate isomerase

Structural highlights

2icj is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.7Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

IDI1_HUMAN Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

↑ Hahn FM, Xuan JW, Chambers AF, Poulter CD. Human isopentenyl diphosphate: dimethylallyl diphosphate isomerase: overproduction, purification, and characterization. Arch Biochem Biophys. 1996 Aug 1;332(1):30-4. PMID:8806705 doi:http://dx.doi.org/S0003-9861(96)90312-4

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OCA

[1] Hahn FM, Xuan JW, Chambers AF, Poulter CD. Human isopentenyl diphosphate: dimethylallyl diphosphate isomerase: overproduction, purification, and characterization. Arch Biochem Biophys. 1996 Aug 1;332(1):30-4. PMID:8806705 doi:http://dx.doi.org/S0003-9861(96)90312-4

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