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Magnesium in PDB 4u9l: Structure of A Membrane Protein

Protein crystallography data

The structure of Structure of A Membrane Protein, PDB code: 4u9l was solved by H.Takeda, M.Hattori, T.Nishizawa, K.Yamashita, S.T.A.Shah, M.Caffrey, A.D.Maturana, R.Ishitani, O.Nureki, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.42 / 2.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 62.529, 70.165, 102.644, 90.00, 90.00, 90.00
R / Rfree (%) 22.4 / 26.3

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of A Membrane Protein (pdb code 4u9l). 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 Structure of A Membrane Protein, PDB code: 4u9l:

Magnesium binding site 1 out of 1 in 4u9l

Go back to Magnesium Binding Sites List in 4u9l
Magnesium binding site 1 out of 1 in the Structure of A Membrane Protein


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of A Membrane Protein within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg501

b:38.3
occ:1.00
O A:HOH606 2.0 30.3 1.0
O B:HOH609 2.1 29.7 1.0
O A:HOH607 2.1 31.4 1.0
O B:HOH607 2.2 51.4 1.0
O B:HOH606 2.2 33.7 1.0
O A:HOH605 2.2 34.9 1.0
O B:HOH608 3.6 34.0 1.0
O A:HOH609 3.7 40.8 1.0
OD2 B:ASP432 4.0 59.5 1.0
O A:HOH608 4.0 28.4 1.0
OD1 B:ASP432 4.0 51.7 1.0
O B:HOH610 4.1 26.2 1.0
O A:HOH612 4.2 40.8 1.0
OD2 A:ASP432 4.4 48.3 1.0
CG B:ASP432 4.4 51.5 1.0
OD1 A:ASP432 4.5 44.4 1.0
CA A:GLY325 4.6 26.6 1.0
O A:HOH610 4.6 37.9 1.0
O B:HOH614 4.7 57.7 1.0
CB B:ALA428 4.8 36.8 1.0
CG A:ASP432 4.9 43.4 1.0
CB A:ALA428 4.9 30.9 1.0
CA B:GLY325 4.9 32.9 1.0

Reference:

H.Takeda, M.Hattori, T.Nishizawa, K.Yamashita, S.T.Shah, M.Caffrey, A.D.Maturana, R.Ishitani, O.Nureki. Structural Basis For Ion Selectivity Revealed By High-Resolution Crystal Structure of Mg(2+) Channel Mgte Nat Commun V. 5 5374 2014.
ISSN: ESSN 2041-1723
PubMed: 25367295
DOI: 10.1038/NCOMMS6374
Page generated: Tue Aug 20 04:33:29 2024

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