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Magnesium in PDB 7z00: Crystal Structure of Vibrio Alkaline Phosphatase in 1.0 M Kbr

Protein crystallography data

The structure of Crystal Structure of Vibrio Alkaline Phosphatase in 1.0 M Kbr, PDB code: 7z00 was solved by S.Markusson, J.G.Hjorleifsson, P.Kursula, B.Asgeirsson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.39 / 2.60
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 99.25, 118.12, 84.4, 90, 90, 90
R / Rfree (%) 24.2 / 29.1

Other elements in 7z00:

The structure of Crystal Structure of Vibrio Alkaline Phosphatase in 1.0 M Kbr also contains other interesting chemical elements:

Bromine (Br) 1 atom
Zinc (Zn) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Vibrio Alkaline Phosphatase in 1.0 M Kbr (pdb code 7z00). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Vibrio Alkaline Phosphatase in 1.0 M Kbr, PDB code: 7z00:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 7z00

Go back to Magnesium Binding Sites List in 7z00
Magnesium binding site 1 out of 2 in the Crystal Structure of Vibrio Alkaline Phosphatase in 1.0 M Kbr


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 Vibrio Alkaline Phosphatase in 1.0 M Kbr within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg604

b:62.5
occ:1.00
HG1 B:THR118 2.2 81.5 1.0
OG1 B:THR118 2.5 67.8 1.0
OD1 B:ASP12 2.6 63.4 1.0
OE2 B:GLU268 2.6 63.7 1.0
CG B:ASP12 2.9 65.6 1.0
OD2 B:ASP12 3.3 68.6 1.0
H B:THR118 3.4 84.3 1.0
HB2 B:ASP12 3.5 75.7 1.0
HB B:THR118 3.5 80.6 1.0
ND1 B:HIS116 3.5 68.1 1.0
CB B:THR118 3.6 67.1 1.0
CD B:GLU268 3.6 66.4 1.0
CB B:ASP12 3.7 63.0 1.0
HB3 B:SER65 3.7 86.2 1.0
OG B:SER65 3.7 71.2 1.0
O4 B:PO4606 3.8 66.3 1.0
HE1 B:HIS116 3.8 80.9 1.0
HB3 B:ASP12 3.9 75.7 1.0
OE1 B:GLU268 4.0 66.1 1.0
CE1 B:HIS116 4.0 67.3 1.0
N B:THR118 4.1 70.2 1.0
CB B:SER65 4.2 71.7 1.0
HA3 B:GLY270 4.3 79.9 1.0
HA2 B:GLY270 4.3 79.9 1.0
HG1 B:THR112 4.3 78.5 1.0
HB3 B:ALA117 4.3 87.3 1.0
HB2 B:SER65 4.3 86.2 1.0
HG21 B:THR112 4.3 83.4 1.0
ZN B:ZN602 4.4 64.9 1.0
HB3 B:HIS116 4.4 84.8 1.0
HG21 B:THR118 4.5 76.8 1.0
CA B:THR118 4.5 68.8 1.0
O B:GLY270 4.5 66.8 1.0
O3 B:PO4606 4.6 64.0 1.0
CG B:HIS116 4.6 71.5 1.0
CG2 B:THR118 4.7 63.9 1.0
H B:ALA117 4.7 84.7 1.0
CA B:GLY270 4.7 66.5 1.0
HE1 B:TRP274 4.7 85.8 1.0
HB3 B:ASP273 4.8 76.2 1.0
HD2 B:PRO119 4.8 85.1 1.0
P B:PO4606 4.8 66.8 1.0
HH22 B:ARG129 4.8 70.2 1.0
CG B:GLU268 4.9 65.2 1.0
HD3 B:PRO119 4.9 85.1 1.0
HA B:THR118 4.9 82.7 1.0
HG3 B:GLU268 4.9 78.3 1.0

Magnesium binding site 2 out of 2 in 7z00

Go back to Magnesium Binding Sites List in 7z00
Magnesium binding site 2 out of 2 in the Crystal Structure of Vibrio Alkaline Phosphatase in 1.0 M Kbr


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Vibrio Alkaline Phosphatase in 1.0 M Kbr within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg605

b:73.3
occ:1.00
O B:SER485 2.5 70.0 1.0
HB3 B:LYS486 3.1 90.1 1.0
C B:SER485 3.7 67.8 1.0
HB3 B:SER485 3.9 80.3 1.0
CB B:LYS486 4.0 75.0 1.0
HA B:LYS486 4.0 84.8 1.0
CA B:LYS486 4.4 70.6 1.0
HB2 B:LYS486 4.4 90.1 1.0
N B:LYS486 4.4 68.6 1.0
HD23 B:LEU482 4.5 84.5 1.0
CB B:SER485 4.7 66.8 1.0
CA B:SER485 4.7 68.6 1.0
HD21 B:LEU482 4.8 84.5 1.0
HD2 B:LYS486 4.9 91.2 1.0
HG2 B:LYS486 4.9 86.3 1.0

Reference:

S.Markusson, J.G.Hjorleifsson, P.Kursula, B.Asgeirsson. Structural Characterization of Functionally Important Chloride Binding Sites in the Marine Vibrio Alkaline Phosphatase. Biochemistry V. 61 2248 2022.
ISSN: ISSN 0006-2960
PubMed: 36194497
DOI: 10.1021/ACS.BIOCHEM.2C00438
Page generated: Thu Oct 3 16:11:27 2024

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