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Magnesium in PDB 1xmv: E. Coli Reca in Complex with Mgadp

Protein crystallography data

The structure of E. Coli Reca in Complex with Mgadp, PDB code: 1xmv was solved by C.E.Bell, X.Xing, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.14 / 1.90
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 100.509, 100.509, 82.227, 90.00, 90.00, 120.00
R / Rfree (%) 20.2 / 23.5

Magnesium Binding Sites:

The binding sites of Magnesium atom in the E. Coli Reca in Complex with Mgadp (pdb code 1xmv). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the E. Coli Reca in Complex with Mgadp, PDB code: 1xmv:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 1xmv

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Magnesium binding site 1 out of 4 in the E. Coli Reca in Complex with Mgadp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of E. Coli Reca in Complex with Mgadp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg701

b:28.7
occ:1.00
OG1 A:THR73 1.9 33.4 1.0
O3B A:ADP400 2.0 32.6 1.0
O A:HOH542 2.0 38.9 1.0
O A:HOH513 2.1 46.1 1.0
O A:HOH568 2.3 38.9 1.0
O A:HOH511 2.4 34.0 1.0
CB A:THR73 3.0 31.2 1.0
PB A:ADP400 3.3 32.1 1.0
O1B A:ADP400 3.5 36.3 1.0
O1A A:ADP400 3.7 29.5 1.0
OD2 A:ASP144 3.8 48.3 1.0
O A:HOH567 3.9 49.6 1.0
N A:THR73 4.0 29.7 1.0
CG2 A:THR73 4.0 43.0 1.0
O A:HOH515 4.0 43.7 1.0
CA A:THR73 4.0 29.2 1.0
O A:HOH433 4.1 39.2 1.0
O3A A:ADP400 4.2 29.4 1.0
PA A:ADP400 4.4 31.3 1.0
O2B A:ADP400 4.4 27.3 1.0
O A:HOH578 4.6 56.8 1.0
CG A:ASP144 4.7 42.2 1.0
O A:HOH465 4.8 40.1 1.0
O2A A:ADP400 4.8 34.0 1.0
OD1 A:ASP144 4.8 39.9 1.0
O A:HOH543 4.8 65.4 1.0

Magnesium binding site 2 out of 4 in 1xmv

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Magnesium binding site 2 out of 4 in the E. Coli Reca in Complex with Mgadp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of E. Coli Reca in Complex with Mgadp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg702

b:42.0
occ:1.00
O A:LYS23 2.1 34.2 1.0
OE2 A:GLU18 2.3 47.2 1.0
O A:ILE26 2.5 28.1 1.0
O A:HOH484 2.5 44.7 1.0
O A:HOH561 2.8 42.4 1.0
C A:LYS23 3.3 34.9 1.0
CD A:GLU18 3.5 42.6 1.0
CG A:MET27 3.6 33.3 1.0
C A:ILE26 3.6 29.2 1.0
CG A:GLU18 4.0 31.0 1.0
CA A:LYS23 4.1 37.2 1.0
CA A:MET27 4.3 29.4 1.0
N A:GLY24 4.3 32.1 1.0
CE A:LYS23 4.3 39.0 1.0
OE1 A:GLU31 4.3 50.1 1.0
CB A:MET27 4.3 29.9 1.0
NZ A:LYS23 4.4 40.6 1.0
CA A:GLY24 4.4 29.7 1.0
O A:HOH580 4.4 55.7 1.0
N A:MET27 4.4 22.4 1.0
N A:ILE26 4.4 25.7 1.0
OE1 A:GLU18 4.5 42.5 1.0
CB A:LYS23 4.6 37.3 1.0
O A:HOH496 4.6 57.8 1.0
CA A:ILE26 4.7 28.1 1.0
CG2 A:ILE26 4.8 25.3 1.0
CD A:LYS23 4.8 35.2 1.0
C A:GLY24 4.8 29.9 1.0
SD A:MET27 4.8 41.2 1.0
OE2 A:GLU31 4.9 44.2 1.0
N A:SER25 4.9 27.0 1.0

Magnesium binding site 3 out of 4 in 1xmv

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Magnesium binding site 3 out of 4 in the E. Coli Reca in Complex with Mgadp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of E. Coli Reca in Complex with Mgadp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg703

b:59.4
occ:1.00
OD1 A:ASP120 3.5 47.5 1.0
O A:HOH430 4.4 36.5 1.0
CG A:ASP120 4.4 52.5 1.0
OD2 A:ASP120 4.8 53.9 1.0

Magnesium binding site 4 out of 4 in 1xmv

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Magnesium binding site 4 out of 4 in the E. Coli Reca in Complex with Mgadp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of E. Coli Reca in Complex with Mgadp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg704

b:68.6
occ:1.00
O A:GLN20 3.7 40.6 1.0
C A:PHE21 4.3 37.2 1.0
O A:LYS19 4.3 34.4 1.0
N A:GLY22 4.3 39.9 1.0
C A:GLN20 4.3 40.0 1.0
CA A:PHE21 4.5 37.4 1.0
O A:PHE21 4.6 39.8 1.0
N A:PHE21 4.7 33.9 1.0
CA A:GLY22 4.8 32.0 1.0

Reference:

X.Xing, C.E.Bell. Crystal Structures of Escherichia Coli Reca in Complex with Mgadp and Mnamp-Pnp(,). Biochemistry V. 43 16142 2004.
ISSN: ISSN 0006-2960
PubMed: 15610008
DOI: 10.1021/BI048165Y
Page generated: Mon Dec 14 07:04:40 2020

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