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Magnesium in PDB 2vm8: Human Crmp-2 Crystallised in the Presence of Mg

Protein crystallography data

The structure of Human Crmp-2 Crystallised in the Presence of Mg, PDB code: 2vm8 was solved by P.Kursula, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 86.510, 126.240, 209.750, 90.00, 90.00, 90.00
R / Rfree (%) 25.6 / 32.5

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Human Crmp-2 Crystallised in the Presence of Mg (pdb code 2vm8). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Human Crmp-2 Crystallised in the Presence of Mg, PDB code: 2vm8:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 2vm8

Go back to Magnesium Binding Sites List in 2vm8
Magnesium binding site 1 out of 3 in the Human Crmp-2 Crystallised in the Presence of Mg


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Human Crmp-2 Crystallised in the Presence of Mg within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1491

b:44.8
occ:1.00
O A:HOH2061 2.2 20.5 1.0
O A:HOH2322 2.3 29.4 1.0
O A:HOH2062 2.3 24.2 1.0
O A:HOH2317 2.5 22.6 1.0
OE1 A:GLU353 3.4 30.3 1.0
NE2 A:GLN81 3.6 35.0 1.0
CD A:GLN81 3.7 35.5 1.0
OD1 A:ASP80 3.9 33.4 1.0
OD2 A:ASP80 3.9 32.0 1.0
O A:ILE351 4.0 24.1 1.0
CD A:GLU353 4.0 24.7 1.0
CG A:GLN81 4.1 34.7 1.0
O A:HOH2065 4.2 26.5 1.0
OE1 A:GLN81 4.2 36.6 1.0
O A:HOH2318 4.3 33.4 1.0
CG A:ASP80 4.3 29.8 1.0
CA A:PRO352 4.4 20.3 1.0
CG A:GLU353 4.5 22.1 1.0
N A:GLU353 4.5 20.8 1.0
O A:THR349 4.6 22.1 1.0
O A:HOH2320 4.7 34.6 1.0
OE2 A:GLU353 4.7 28.7 1.0
C A:ILE351 4.7 21.1 1.0
O A:HOH2319 4.9 28.3 1.0
N A:PRO352 5.0 21.3 1.0

Magnesium binding site 2 out of 3 in 2vm8

Go back to Magnesium Binding Sites List in 2vm8
Magnesium binding site 2 out of 3 in the Human Crmp-2 Crystallised in the Presence of Mg


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Human Crmp-2 Crystallised in the Presence of Mg within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1491

b:47.4
occ:1.00
O B:HOH2292 2.0 36.8 1.0
O B:HOH2293 2.2 15.0 1.0
O B:HOH2059 2.5 10.3 1.0
O B:HOH2058 2.7 12.5 1.0
OE1 B:GLU353 3.5 20.6 1.0
NH2 B:ARG173 3.8 26.2 0.5
O B:THR349 3.9 13.1 1.0
O B:HOH2291 3.9 12.8 1.0
OD2 B:ASP80 4.3 21.3 1.0
NH1 B:ARG173 4.3 24.0 0.5
CD B:GLU353 4.4 14.0 1.0
CZ B:ARG173 4.4 23.7 0.5
OD1 B:ASP80 4.4 10.8 1.0
NE2 B:GLN81 4.5 30.5 1.0
O B:ILE351 4.6 12.3 1.0
CG B:ASP80 4.8 19.7 1.0

Magnesium binding site 3 out of 3 in 2vm8

Go back to Magnesium Binding Sites List in 2vm8
Magnesium binding site 3 out of 3 in the Human Crmp-2 Crystallised in the Presence of Mg


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Human Crmp-2 Crystallised in the Presence of Mg within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg1491

b:32.1
occ:1.00
O C:HOH2374 1.9 19.2 1.0
O C:HOH2375 2.4 8.4 1.0
O C:HOH2076 2.6 38.2 1.0
OE1 C:GLN81 3.5 37.0 1.0
O C:HOH2373 3.5 39.8 1.0
O C:THR349 3.6 23.4 1.0
CD C:GLN81 3.8 36.2 1.0
O C:ILE351 3.8 10.1 1.0
NE2 C:GLN81 4.1 40.4 1.0
OE1 C:GLU353 4.1 15.3 1.0
O C:HOH2075 4.2 13.0 1.0
CD C:GLU353 4.4 15.4 1.0
C C:LEU350 4.4 15.1 1.0
O C:LEU350 4.4 17.5 1.0
CA C:LEU350 4.5 15.0 1.0
C C:THR349 4.5 18.9 1.0
CG C:GLN81 4.6 36.0 1.0
C C:ILE351 4.6 12.7 1.0
OD2 C:ASP80 4.6 32.2 1.0
O C:HOH2372 4.6 10.7 1.0
OD1 C:ASP80 4.7 32.6 1.0
OE2 C:GLU353 4.7 17.9 1.0
CG C:GLU353 4.8 12.6 1.0
CA C:PRO352 4.8 11.8 1.0
N C:ILE351 4.9 14.1 1.0
N C:GLU353 4.9 15.3 1.0
N C:LEU350 4.9 17.4 1.0
O C:HOH2216 4.9 47.1 1.0

Reference:

V.Majava, N.Loytynoja, W.Q.Chen, G.Lubec, P.Kursula. Crystal and Solution Structure, Stability and Post- Translational Modifications of Collapsin Response Mediator Protein 2. Febs J. V. 275 4583 2008.
ISSN: ISSN 1742-464X
PubMed: 18699782
DOI: 10.1111/J.1742-4658.2008.06601.X
Page generated: Wed Aug 14 05:16:58 2024

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