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Magnesium in PDB 1t1s: Crystal Structure of the Reductoisomerase Complexed with A Bisphosphonate

Enzymatic activity of Crystal Structure of the Reductoisomerase Complexed with A Bisphosphonate

All present enzymatic activity of Crystal Structure of the Reductoisomerase Complexed with A Bisphosphonate:
1.1.1.267;

Protein crystallography data

The structure of Crystal Structure of the Reductoisomerase Complexed with A Bisphosphonate, PDB code: 1t1s was solved by S.Yajima, K.Hara, J.M.Sanders, F.Yin, K.Ohsawa, J.Wiesner, H.Jomaa, E.Oldfield, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.40
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 182.917, 59.246, 86.988, 90.00, 90.00, 90.00
R / Rfree (%) 21.3 / 26

Other elements in 1t1s:

The structure of Crystal Structure of the Reductoisomerase Complexed with A Bisphosphonate also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Reductoisomerase Complexed with A Bisphosphonate (pdb code 1t1s). 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 Crystal Structure of the Reductoisomerase Complexed with A Bisphosphonate, PDB code: 1t1s:

Magnesium binding site 1 out of 1 in 1t1s

Go back to Magnesium Binding Sites List in 1t1s
Magnesium binding site 1 out of 1 in the Crystal Structure of the Reductoisomerase Complexed with A Bisphosphonate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of the Reductoisomerase Complexed with A Bisphosphonate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1002

b:49.1
occ:1.00
 O2 A:CBQ2001 2.1 36.4 0.5
OE2 A:GLU151 2.3 39.0 1.0
OD2 A:ASP149 2.5 42.9 1.0
OE2 A:GLU230 2.7 30.5 1.0
CD A:GLU230 2.7 29.3 1.0
OE1 A:GLU230 3.2 30.3 1.0
CG A:ASP149 3.2 41.4 1.0
CG A:GLU230 3.2 29.5 1.0
CD A:GLU151 3.4 39.7 1.0
CB A:ASP149 3.4 37.3 1.0
P1 A:CBQ2001 3.5 37.0 0.5
CE A:LYS124 3.6 60.9 1.0
NZ A:LYS124 3.6 62.8 1.0
CB A:GLU151 3.9 32.2 1.0
O6 A:CBQ2001 4.0 37.5 0.5
O3 A:CBQ2001 4.1 34.9 0.5
N A:GLU151 4.1 30.2 1.0
CG A:GLU151 4.1 38.0 1.0
OD1 A:ASP149 4.3 48.2 1.0
O1 A:CBQ2001 4.3 37.0 0.5
OE1 A:GLU151 4.3 43.5 1.0
CB A:GLU230 4.4 29.1 1.0
ND1 A:HIS152 4.4 25.8 1.0
C1 A:CBQ2001 4.5 37.0 0.5
CE1 A:HIS152 4.5 26.9 1.0
C A:ASP149 4.6 35.0 1.0
CA A:ASP149 4.6 35.8 1.0
CA A:GLU151 4.6 31.1 1.0
N1 A:CBQ2001 4.6 36.5 0.5
N A:SER150 4.7 34.6 1.0
N A:HIS152 4.8 26.6 1.0
P2 A:CBQ2001 4.9 40.1 0.5
CD A:LYS124 4.9 58.3 1.0
CG A:HIS152 5.0 26.5 1.0

Reference:

S.Yajima, K.Hara, J.M.Sanders, F.Yin, K.Ohsawa, J.Wiesner, H.Jomaa, E.Oldfield. Crystallographic Structures of Two Bisphosphonate:1-Deoxyxylulose-5-Phosphate Reductoisomerase Complexes J.Am.Chem.Soc. V. 126 10824 2004.
ISSN: ISSN 0002-7863
PubMed: 15339150
DOI: 10.1021/JA040126M
Page generated: Tue Aug 13 14:25:00 2024

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