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Magnesium in PDB 2bz0: Crystal Structure of E. Coli Gtp Cyclohydrolase II in Complex with Gtp Analogue, Gmpcpp, and Zinc

Enzymatic activity of Crystal Structure of E. Coli Gtp Cyclohydrolase II in Complex with Gtp Analogue, Gmpcpp, and Zinc

All present enzymatic activity of Crystal Structure of E. Coli Gtp Cyclohydrolase II in Complex with Gtp Analogue, Gmpcpp, and Zinc:
3.5.4.25;

Protein crystallography data

The structure of Crystal Structure of E. Coli Gtp Cyclohydrolase II in Complex with Gtp Analogue, Gmpcpp, and Zinc, PDB code: 2bz0 was solved by J.Ren, M.Kotaka, M.Lockyer, H.K.Lamb, A.R.Hawkins, D.K.Stammers, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.03 / 2.6
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 99.080, 99.080, 96.290, 90.00, 90.00, 90.00
R / Rfree (%) 21 / 26

Other elements in 2bz0:

The structure of Crystal Structure of E. Coli Gtp Cyclohydrolase II in Complex with Gtp Analogue, Gmpcpp, and Zinc also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of E. Coli Gtp Cyclohydrolase II in Complex with Gtp Analogue, Gmpcpp, and Zinc (pdb code 2bz0). 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 E. Coli Gtp Cyclohydrolase II in Complex with Gtp Analogue, Gmpcpp, and Zinc, PDB code: 2bz0:

Magnesium binding site 1 out of 1 in 2bz0

Go back to Magnesium Binding Sites List in 2bz0
Magnesium binding site 1 out of 1 in the Crystal Structure of E. Coli Gtp Cyclohydrolase II in Complex with Gtp Analogue, Gmpcpp, and Zinc


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 E. Coli Gtp Cyclohydrolase II in Complex with Gtp Analogue, Gmpcpp, and Zinc within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1175

b:53.5
occ:1.00
 ND1 A:HIS51 3.4 41.8 1.0
CE1 A:HIS51 3.5 52.7 1.0
O A:SER52 3.5 46.0 1.0
O2B A:G2P1176 3.5 0.3 1.0
C5' A:G2P1176 3.5 71.7 1.0
N A:SER52 3.5 30.4 1.0
C3A A:G2P1176 3.9 0.5 1.0
OE1 A:GLN70 4.0 95.9 1.0
NE2 A:HIS51 4.0 39.1 1.0
CG A:HIS51 4.0 32.3 1.0
NH2 A:ARG49 4.1 35.3 1.0
CA A:SER52 4.3 37.4 1.0
C A:SER52 4.3 31.4 1.0
O5' A:G2P1176 4.3 0.9 1.0
CB A:SER52 4.3 35.2 1.0
CD2 A:HIS51 4.4 34.2 1.0
CA A:HIS51 4.4 27.7 1.0
C A:HIS51 4.4 31.7 1.0
PB A:G2P1176 4.5 0.2 1.0
SG A:CYS67 4.5 63.0 1.0
C3' A:G2P1176 4.5 83.7 1.0
C4' A:G2P1176 4.6 76.0 1.0
CB A:HIS51 4.8 26.2 1.0
CB A:CYS67 4.9 55.3 1.0

Reference:

J.Ren, M.Kotaka, M.Lockyer, H.K.Lamb, A.R.Hawkins, D.K.Stammers. Gtp Cyclohydrolase II Structure and Mechanism. J.Biol.Chem. V. 280 36912 2005.
ISSN: ISSN 0021-9258
PubMed: 16115872
DOI: 10.1074/JBC.M507725200
Page generated: Tue Aug 13 22:07:05 2024

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