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Magnesium in PDB 4umv: Crystal Structure of A Zinc-Transporting Pib-Type Atpase in the E2P State

Enzymatic activity of Crystal Structure of A Zinc-Transporting Pib-Type Atpase in the E2P State

All present enzymatic activity of Crystal Structure of A Zinc-Transporting Pib-Type Atpase in the E2P State:
3.6.3.5;

Protein crystallography data

The structure of Crystal Structure of A Zinc-Transporting Pib-Type Atpase in the E2P State, PDB code: 4umv was solved by K.T.Wang, O.Sitsel, G.Meloni, H.E.Autzen, M.Andersson, T.Klymchuk, A.M.Nielsen, D.C.Rees, P.Nissen, P.Gourdon, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.082 / 3.20
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 54.462, 60.972, 141.523, 90.00, 95.99, 90.00
R / Rfree (%) 21.85 / 28.14

Other elements in 4umv:

The structure of Crystal Structure of A Zinc-Transporting Pib-Type Atpase in the E2P State also contains other interesting chemical elements:

Fluorine (F) 3 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of A Zinc-Transporting Pib-Type Atpase in the E2P State (pdb code 4umv). 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 Crystal Structure of A Zinc-Transporting Pib-Type Atpase in the E2P State, PDB code: 4umv:

Magnesium binding site 1 out of 1 in 4umv

Go back to Magnesium Binding Sites List in 4umv
Magnesium binding site 1 out of 1 in the Crystal Structure of A Zinc-Transporting Pib-Type Atpase in the E2P State


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 A Zinc-Transporting Pib-Type Atpase in the E2P State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1731

b:71.2
occ:1.00
 OD2 A:ASP628 1.3 51.2 1.0
CG A:ASP628 1.7 49.8 1.0
OD1 A:ASP628 1.9 43.5 1.0
F1 A:BEF1732 1.9 64.7 1.0
O A:THR438 2.4 41.6 1.0
BE A:BEF1732 2.9 75.8 1.0
OD2 A:ASP436 3.1 30.4 1.0
F2 A:BEF1732 3.2 96.1 1.0
CB A:ASP628 3.2 50.1 1.0
N A:GLY629 3.5 38.2 1.0
C A:THR438 3.6 35.1 1.0
CA A:ASP628 4.1 33.8 1.0
OD2 A:ASP632 4.2 51.9 1.0
CA A:GLY629 4.2 42.7 1.0
CG A:ASP436 4.2 33.6 1.0
F3 A:BEF1732 4.2 74.2 1.0
O A:SER285 4.2 32.5 1.0
N A:ASP628 4.3 36.0 1.0
C A:ASP628 4.3 34.4 1.0
CB A:THR438 4.3 27.7 1.0
CA A:THR438 4.5 29.9 1.0
CG2 A:THR440 4.6 26.1 1.0
N A:GLY439 4.6 34.6 1.0
CA A:GLY439 4.7 37.1 1.0
OD1 A:ASP436 4.8 38.0 1.0
OD1 A:ASN631 4.8 35.8 1.0
N A:THR438 4.8 32.4 1.0
CA A:GLY289 4.9 34.1 1.0
N A:THR440 5.0 32.8 1.0

Reference:

K.Wang, O.Sitsel, G.Meloni, H.E.Autzen, M.Andersson, T.Klymchuk, A.M.Nielsen, D.C.Rees, P.Nissen, P.Gourdon. Structure and Mechanism of Zn(2+)-Transporting P-Type Atpases. Nature V. 514 518 2014.
ISSN: ESSN 0028-0836
PubMed: 25132545
DOI: 10.1038/NATURE13618
Page generated: Tue Aug 20 04:51:30 2024

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