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Magnesium in PDB 1bl5: Isocitrate Dehydrogenase From E. Coli Single Turnover Laue Structure of Rate-Limited Product Complex, 10 Msec Time Resolution

Enzymatic activity of Isocitrate Dehydrogenase From E. Coli Single Turnover Laue Structure of Rate-Limited Product Complex, 10 Msec Time Resolution

All present enzymatic activity of Isocitrate Dehydrogenase From E. Coli Single Turnover Laue Structure of Rate-Limited Product Complex, 10 Msec Time Resolution:
1.1.1.42;

Protein crystallography data

The structure of Isocitrate Dehydrogenase From E. Coli Single Turnover Laue Structure of Rate-Limited Product Complex, 10 Msec Time Resolution, PDB code: 1bl5 was solved by B.L.Stoddard, B.Cohen, M.Brubaker, 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 / 2.50
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 106.100, 106.100, 151.800, 90.00, 90.00, 90.00
R / Rfree (%) 22.2 / 27.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Isocitrate Dehydrogenase From E. Coli Single Turnover Laue Structure of Rate-Limited Product Complex, 10 Msec Time Resolution (pdb code 1bl5). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Isocitrate Dehydrogenase From E. Coli Single Turnover Laue Structure of Rate-Limited Product Complex, 10 Msec Time Resolution, PDB code: 1bl5:

Magnesium binding site 1 out of 1 in 1bl5

Go back to Magnesium Binding Sites List in 1bl5
Magnesium binding site 1 out of 1 in the Isocitrate Dehydrogenase From E. Coli Single Turnover Laue Structure of Rate-Limited Product Complex, 10 Msec Time Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Isocitrate Dehydrogenase From E. Coli Single Turnover Laue Structure of Rate-Limited Product Complex, 10 Msec Time Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg418

b:9.8
occ:1.00
 O5 A:AKG1 2.1 12.6 1.0
O2 A:AKG1 2.2 14.7 1.0
OD1 A:ASP307 2.4 1.8 1.0
C2 A:AKG1 3.0 11.6 1.0
C1 A:AKG1 3.1 13.0 1.0
CG A:ASP307 3.5 2.5 1.0
OD1 A:ASP311 3.5 9.6 1.0
NH1 A:ARG129 3.9 4.8 1.0
OD2 A:ASP307 4.1 4.1 1.0
O A:ASP307 4.1 5.9 1.0
O1 A:AKG1 4.2 13.0 1.0
CG A:ASP311 4.4 8.8 1.0
C3 A:AKG1 4.4 11.8 1.0
NH2 A:ARG129 4.4 1.9 1.0
NH1 A:ARG153 4.5 1.8 1.0
OD2 A:ASP311 4.6 11.8 1.0
CZ A:ARG129 4.7 4.3 1.0
CB A:ASP307 4.7 1.8 1.0
CA A:ASP307 4.8 1.8 1.0
C A:ASP307 4.8 3.0 1.0

Reference:

B.L.Stoddard, B.E.Cohen, M.Brubaker, A.D.Mesecar, D.E.Koshland Jr.. Millisecond Laue Structures of An Enzyme-Product Complex Using Photocaged Substrate Analogs. Nat.Struct.Biol. V. 5 891 1998.
ISSN: ISSN 1072-8368
PubMed: 9783749
DOI: 10.1038/2331
Page generated: Tue Aug 13 02:13:24 2024

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