Calcium in PDB 1ai2: Isocitrate Dehydrogenase Complexed with Isocitrate, Nadp+, and Calcium (Flash-Cooled)

All present enzymatic activity of Isocitrate Dehydrogenase Complexed with Isocitrate, Nadp+, and Calcium (Flash-Cooled):
1.1.1.42;

The structure of Isocitrate Dehydrogenase Complexed with Isocitrate, Nadp+, and Calcium (Flash-Cooled), PDB code: 1ai2 was solved by B.L.Stoddard, A.Mesecar, D.E.Koshland Junior, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.90
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	102.300, 102.300, 150.500, 90.00, 90.00, 90.00
R / Rfree (%)	19.1 / 21.5

The binding sites of Calcium atom in the Isocitrate Dehydrogenase Complexed with Isocitrate, Nadp+, and Calcium (Flash-Cooled) (pdb code 1ai2). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Isocitrate Dehydrogenase Complexed with Isocitrate, Nadp+, and Calcium (Flash-Cooled), PDB code: 1ai2:

Calcium binding site 1 out of 1 in the Isocitrate Dehydrogenase Complexed with Isocitrate, Nadp+, and Calcium (Flash-Cooled)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Isocitrate Dehydrogenase Complexed with Isocitrate, Nadp+, and Calcium (Flash-Cooled) within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca418 b:30.2 occ:1.00 CA A:ICA418 0.0 30.2 1.0 OD2 A:ASP311 2.3 21.5 1.0 O A:HOH458 2.5 45.4 1.0 O7 A:ICA418 2.5 36.3 1.0 O2 A:ICA418 2.5 38.7 1.0 O A:HOH459 2.6 35.7 1.0 OD1 A:ASP307 2.7 15.5 1.0 OD1 A:ASP311 2.9 18.8 1.0 CG A:ASP311 3.0 20.5 1.0 C1 A:ICA418 3.3 34.5 0.0 C2 A:ICA418 3.3 32.3 1.0 CG A:ASP307 3.7 14.5 1.0 OD2 A:ASP307 4.1 14.6 1.0 CB A:ASP311 4.4 11.5 1.0 O1 A:ICA418 4.5 35.7 1.0 C4N A:NAP417 4.5 38.8 1.0 O A:ASP307 4.5 11.7 1.0 C3 A:ICA418 4.6 33.3 1.0 CB A:ASP307 5.0 11.7 1.0 C6 A:ICA418 5.0 35.7 1.0

A.D.Mesecar, B.L.Stoddard, D.E.Koshland Jr.. Orbital Steering in the Catalytic Power of Enzymes: Small Structural Changes with Large Catalytic Consequences. Science V. 277 202 1997.
ISSN: ISSN 0036-8075
PubMed: 9211842
DOI: 10.1126/SCIENCE.277.5323.202