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Magnesium in PDB 1kyr: Crystal Structure of A Cu-Bound Green Fluorescent Protein Zn Biosensor

Protein crystallography data

The structure of Crystal Structure of A Cu-Bound Green Fluorescent Protein Zn Biosensor, PDB code: 1kyr was solved by D.P.Barondeau, C.J.Kassmann, J.A.Tainer, E.D.Getzoff, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 51.166, 62.301, 69.624, 90.00, 90.00, 90.00
R / Rfree (%) 15 / 21.9

Other elements in 1kyr:

The structure of Crystal Structure of A Cu-Bound Green Fluorescent Protein Zn Biosensor also contains other interesting chemical elements:

Copper (Cu) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of A Cu-Bound Green Fluorescent Protein Zn Biosensor (pdb code 1kyr). 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 A Cu-Bound Green Fluorescent Protein Zn Biosensor, PDB code: 1kyr:

Magnesium binding site 1 out of 1 in 1kyr

Go back to Magnesium Binding Sites List in 1kyr
Magnesium binding site 1 out of 1 in the Crystal Structure of A Cu-Bound Green Fluorescent Protein Zn Biosensor


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 A Cu-Bound Green Fluorescent Protein Zn Biosensor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg303

b:22.7
occ:1.00
O A:HOH1118 2.0 31.2 1.0
OE2 A:GLU142 2.1 22.2 1.0
O A:HOH1119 2.1 31.5 1.0
CD A:GLU142 3.1 23.3 1.0
OE1 A:GLU142 3.3 26.0 1.0
O A:ILE171 4.2 17.9 1.0
CA A:GLY174 4.3 21.9 1.0
O A:HOH1177 4.3 26.7 1.0
CG A:GLU142 4.4 21.4 1.0
N A:GLY174 4.6 21.6 1.0
O A:GLU172 4.7 24.8 1.0
CB A:ASN170 4.9 17.6 1.0

Reference:

D.P.Barondeau, C.J.Kassmann, J.A.Tainer, E.D.Getzoff. Structural Chemistry of A Green Fluorescent Protein Zn Biosensor. J.Am.Chem.Soc. V. 124 3522 2002.
ISSN: ISSN 0002-7863
PubMed: 11929238
DOI: 10.1021/JA0176954
Page generated: Mon Dec 14 06:22:41 2020

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