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Magnesium in PDB 5kue: Human Semet Incorporated I141M/L146M Mitochondrial Calcium Uniporter (Residues 72-189) Crystal Structure with Magnesium

Protein crystallography data

The structure of Human Semet Incorporated I141M/L146M Mitochondrial Calcium Uniporter (Residues 72-189) Crystal Structure with Magnesium, PDB code: 5kue was solved by C.Y.M.Mok, S.K.Lee, M.S.Junop, P.B.Stathopulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.44 / 1.50
Space group P 65
Cell size a, b, c (Å), α, β, γ (°) 55.500, 55.500, 69.020, 90.00, 90.00, 120.00
R / Rfree (%) 20.1 / 21.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Human Semet Incorporated I141M/L146M Mitochondrial Calcium Uniporter (Residues 72-189) Crystal Structure with Magnesium (pdb code 5kue). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Human Semet Incorporated I141M/L146M Mitochondrial Calcium Uniporter (Residues 72-189) Crystal Structure with Magnesium, PDB code: 5kue:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 5kue

Go back to Magnesium Binding Sites List in 5kue
Magnesium binding site 1 out of 2 in the Human Semet Incorporated I141M/L146M Mitochondrial Calcium Uniporter (Residues 72-189) Crystal Structure with Magnesium


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Human Semet Incorporated I141M/L146M Mitochondrial Calcium Uniporter (Residues 72-189) Crystal Structure with Magnesium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg201

b:22.7
occ:1.00
O A:LEU144 2.8 14.5 1.0
O A:HOH323 2.8 26.8 1.0
O A:HOH369 2.8 20.4 1.0
O A:ASP148 2.8 14.0 1.0
O A:ASP147 3.1 13.7 1.0
C A:ASP147 3.5 16.0 1.0
CB A:ASP147 3.7 20.8 1.0
C A:ASP148 3.7 15.2 1.0
C A:LEU144 3.8 12.1 1.0
CD1 A:LEU144 3.8 14.6 1.0
CB A:PHE149 3.9 12.7 1.0
CA A:ASP147 3.9 18.3 1.0
N A:ASP147 4.0 17.5 1.0
CA A:LEU144 4.1 12.3 1.0
N A:ASP148 4.2 16.8 1.0
CD1 A:PHE149 4.3 11.2 1.0
N A:PHE149 4.4 12.4 1.0
CG A:LEU144 4.4 13.3 1.0
O1 A:EDO204 4.5 33.0 1.0
CA A:PHE149 4.5 11.3 1.0
CG A:PHE149 4.6 12.8 1.0
CA A:ASP148 4.6 15.5 1.0
O A:LEU143 4.7 14.2 1.0
CB A:LEU144 4.9 12.2 1.0
CG A:ASP147 4.9 29.2 1.0
N A:LEU145 5.0 12.5 1.0

Magnesium binding site 2 out of 2 in 5kue

Go back to Magnesium Binding Sites List in 5kue
Magnesium binding site 2 out of 2 in the Human Semet Incorporated I141M/L146M Mitochondrial Calcium Uniporter (Residues 72-189) Crystal Structure with Magnesium


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Human Semet Incorporated I141M/L146M Mitochondrial Calcium Uniporter (Residues 72-189) Crystal Structure with Magnesium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg202

b:22.9
occ:1.00
O A:VAL85 2.7 12.1 1.0
O A:HOH363 2.8 18.2 1.0
OG A:SER87 2.8 17.6 0.5
OG1 A:THR76 3.0 19.9 1.0
O A:THR76 3.2 13.6 1.0
N A:SER87 3.4 11.5 0.5
N A:SER87 3.4 11.5 0.5
CB A:SER87 3.5 16.9 0.5
CB A:SER87 3.5 16.9 0.5
C A:VAL85 3.6 13.9 1.0
C A:THR76 3.6 14.9 1.0
N A:VAL78 3.7 10.8 1.0
CG2 A:VAL78 3.7 14.7 1.0
O A:HOH303 3.8 18.5 1.0
CB A:VAL78 3.9 13.3 1.0
CB A:THR76 4.0 18.8 1.0
C A:ILE86 4.1 12.0 1.0
CA A:ILE86 4.1 10.8 1.0
N A:VAL77 4.1 13.1 1.0
CA A:SER87 4.1 12.1 0.5
CA A:SER87 4.1 12.1 0.5
CA A:VAL77 4.1 12.7 1.0
CG1 A:VAL85 4.1 11.8 1.0
N A:ILE86 4.2 10.0 1.0
C A:VAL77 4.2 14.9 1.0
CB A:VAL85 4.3 11.4 1.0
CA A:THR76 4.4 15.6 1.0
CA A:VAL78 4.4 11.9 1.0
CA A:VAL85 4.6 11.0 1.0
O A:HOH372 4.6 27.1 1.0
O A:HOH382 4.8 25.5 1.0
OG A:SER87 4.8 19.5 0.5
O A:VAL78 4.8 14.9 1.0

Reference:

S.K.Lee, S.Shanmughapriya, M.C.Mok, Z.Dong, D.Tomar, E.Carvalho, S.Rajan, M.S.Junop, M.Madesh, P.B.Stathopulos. Structural Insights Into Mitochondrial Calcium Uniporter Regulation By Divalent Cations. Cell Chem Biol V. 23 1157 2016.
ISSN: ESSN 2451-9456
PubMed: 27569754
DOI: 10.1016/J.CHEMBIOL.2016.07.012
Page generated: Mon Dec 14 20:38:29 2020

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