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Magnesium in PDB 7osj: Abc Transporter Complex Nosdfyl, Membrane Anchor

Other elements in 7osj:

The structure of Abc Transporter Complex Nosdfyl, Membrane Anchor also contains other interesting chemical elements:

Zinc (Zn) 1 atom
Copper (Cu) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Abc Transporter Complex Nosdfyl, Membrane Anchor (pdb code 7osj). 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 Abc Transporter Complex Nosdfyl, Membrane Anchor, PDB code: 7osj:

Magnesium binding site 1 out of 1 in 7osj

Go back to Magnesium Binding Sites List in 7osj
Magnesium binding site 1 out of 1 in the Abc Transporter Complex Nosdfyl, Membrane Anchor


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Abc Transporter Complex Nosdfyl, Membrane Anchor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg501

b:135.2
occ:1.00
OD2 A:ASP367 2.1 128.8 1.0
O A:TRP358 2.1 128.1 1.0
CD1 A:TRP358 2.4 128.1 1.0
C A:TRP358 2.4 128.1 1.0
CG A:ASP367 2.5 128.8 1.0
CB A:ASP367 2.6 128.8 1.0
CA A:ASP359 2.6 130.6 1.0
N A:ASP359 2.6 130.6 1.0
CG A:TRP358 3.0 128.1 1.0
NE1 A:TRP358 3.1 128.1 1.0
N A:ARG360 3.1 133.6 1.0
C A:ASP359 3.3 130.6 1.0
CA A:TRP358 3.5 128.1 1.0
CB A:TRP358 3.6 128.1 1.0
OD1 A:ASP367 3.6 128.8 1.0
N A:ASP367 3.7 128.8 1.0
CA A:ASP367 3.7 128.8 1.0
CB A:ASP359 3.9 130.6 1.0
CD2 A:TRP358 4.0 128.1 1.0
CE2 A:TRP358 4.0 128.1 1.0
N A:TRP358 4.1 128.1 1.0
OD1 A:ASP359 4.3 130.6 1.0
CA A:ARG360 4.4 133.6 1.0
CG A:ARG360 4.4 133.6 1.0
O A:ASP359 4.5 130.6 1.0
CB A:ARG360 4.5 133.6 1.0
CG A:ASP359 4.6 130.6 1.0
C A:ASP367 4.7 128.8 1.0
C A:GLY366 4.7 127.5 1.0
N A:ILE368 4.9 124.7 1.0

Reference:

C.Muller, L.Zhang, S.Zipfel, A.Topitsch, M.Lutz, J.Eckert, B.Prasser, M.Chami, W.Lu, J.Du, O.Einsle. Molecular Interplay of An Assembly Machinery For Nitrous Oxide Reductase. Nature V. 608 626 2022.
ISSN: ESSN 1476-4687
PubMed: 35896743
DOI: 10.1038/S41586-022-05015-2
Page generated: Thu Oct 3 03:34:38 2024

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