› 2dho

X-ray diffraction
1.6Å resolution

Crystal structure of human IPP isomerase I in space group P212121

Released:
DOI: 10.2210/pdb2dho/pdb
PDB entry 2dho coloured by chain, front view.
PDB entry 2dho coloured by chain, side view.
PDB entry 2dho coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures of human IPP isomerase: new insights into the catalytic mechanism.
Zhang C, Liu L, Xu H, Wei Z, Wang Y, Lin Y, Gong W
J Mol Biol 366 1437-46 (2007)
PMID: 17137593

Function and Biology Details

Reaction catalysed: 
Isopentenyl diphosphate = prenyl diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171834 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Isopentenyl-diphosphate Delta-isomerase 1 Chain: A
Molecule details ›
Chain: A
Length: 235 amino acids
Theoretical weight: 27.37 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13907 (Residues: 1-227; Coverage: 100%)
Gene name: IDI1
Sequence domains: NUDIX domain
Structure domains: Nucleoside Triphosphate Pyrophosphohydrolase

Ligands and Environments

3 bound ligands:
Ligand MN 8 x MN
Ligand NA 2 x NA
Ligand CL 10 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 55.019Å b: 62.947Å c: 74.188Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.173 0.203
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Mechanistic aspects of carotenoid biosynthesis.
Moise et al. (2014)
5 other articles

1 mention without citation

The dipeptidyl peptidase IV inhibitors vildagliptin and K-579 inhibit a phospholipase C: a case of promiscuous scaffolds in proteins.
Chakraborty et al. (2013)