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Magnesium in PDB 3mk1: Refinement of Placental Alkaline Phosphatase Complexed with Nitrophenyl

Enzymatic activity of Refinement of Placental Alkaline Phosphatase Complexed with Nitrophenyl

All present enzymatic activity of Refinement of Placental Alkaline Phosphatase Complexed with Nitrophenyl:
3.1.3.1;

Protein crystallography data

The structure of Refinement of Placental Alkaline Phosphatase Complexed with Nitrophenyl, PDB code: 3mk1 was solved by B.Stec, A.Cheltsov, J.L.Millan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 70.01 / 1.57
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 88.346, 114.573, 106.568, 90.00, 90.00, 90.00
R / Rfree (%) 13.9 / 17.8

Other elements in 3mk1:

The structure of Refinement of Placental Alkaline Phosphatase Complexed with Nitrophenyl also contains other interesting chemical elements:

Zinc (Zn) 3 atoms
Calcium (Ca) 1 atom
Sodium (Na) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Refinement of Placental Alkaline Phosphatase Complexed with Nitrophenyl (pdb code 3mk1). 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 Refinement of Placental Alkaline Phosphatase Complexed with Nitrophenyl, PDB code: 3mk1:

Magnesium binding site 1 out of 1 in 3mk1

Go back to Magnesium Binding Sites List in 3mk1
Magnesium binding site 1 out of 1 in the Refinement of Placental Alkaline Phosphatase Complexed with Nitrophenyl


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Refinement of Placental Alkaline Phosphatase Complexed with Nitrophenyl within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg904

b:14.7
occ:0.20
 ZN A:ZN903 0.0 14.7 0.8
OD2 A:ASP42 2.0 11.4 1.0
OE2 A:GLU311 2.0 12.2 1.0
O A:HOH1003 2.1 12.7 1.0
O A:HOH1005 2.2 12.6 1.0
O A:HOH1004 2.2 12.1 1.0
OG A:SER155 2.2 11.9 1.0
CG A:ASP42 3.0 11.6 1.0
CD A:GLU311 3.0 10.9 1.0
CB A:SER155 3.2 12.3 1.0
OE1 A:GLU311 3.4 12.0 1.0
CB A:ASP42 3.5 11.6 1.0
ND1 A:HIS153 4.1 15.4 1.0
N A:SER155 4.1 12.7 1.0
OD1 A:ASP42 4.1 10.9 1.0
O A:HOH1032 4.1 14.1 1.0
CA A:SER155 4.2 12.3 1.0
OG A:SEP92 4.3 10.5 1.0
CG A:GLU311 4.3 11.8 1.0
O A:GLY313 4.4 12.8 1.0
O2P A:SEP92 4.4 14.5 1.0
CB A:SEP92 4.4 11.7 1.0
O A:HOH1016 4.5 12.2 1.0
CA A:GLY313 4.5 12.0 1.0
ZN A:ZN902 4.7 12.4 1.0
CG2 A:THR149 4.7 11.0 1.0
CE1 A:HIS153 4.7 15.5 1.0
OD2 A:ASP357 4.8 9.4 1.0
CD A:PRO156 4.8 12.3 1.0
OG1 A:THR149 4.9 12.7 1.0
CA A:ASP42 4.9 11.3 1.0
C A:GLY313 4.9 11.9 1.0

Reference:

B.Stec, A.Cheltsov, J.L.Millan. Refined Structures of Placental Alkaline Phosphatase Show A Consistent Pattern of Interactions at the Peripheral Site. Acta Crystallogr.,Sect.F V. 66 866 2010.
ISSN: ESSN 1744-3091
PubMed: 20693656
DOI: 10.1107/S1744309110019767
Page generated: Wed Aug 14 19:20:44 2024

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