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Magnesium in PDB 4q4a: Improved Model of Amp-Pnp Bound TM287/288

Protein crystallography data

The structure of Improved Model of Amp-Pnp Bound TM287/288, PDB code: 4q4a was solved by M.Hohl, M.G.Gruetter, M.A.Seeger, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.93 / 2.60
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 216.330, 84.310, 115.780, 90.00, 91.92, 90.00
R / Rfree (%) 22.6 / 26.8

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Improved Model of Amp-Pnp Bound TM287/288 (pdb code 4q4a). 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 Improved Model of Amp-Pnp Bound TM287/288, PDB code: 4q4a:

Magnesium binding site 1 out of 1 in 4q4a

Go back to Magnesium Binding Sites List in 4q4a
Magnesium binding site 1 out of 1 in the Improved Model of Amp-Pnp Bound TM287/288


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Improved Model of Amp-Pnp Bound TM287/288 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg602

b:1.0
occ:1.00
OE1 A:GLN414 1.9 0.4 1.0
OG A:SER373 2.2 86.2 1.0
N3B A:ANP601 2.6 91.2 1.0
O2B A:ANP601 2.8 85.4 1.0
O2G A:ANP601 2.8 0.2 1.0
CD A:GLN414 2.9 0.1 1.0
PG A:ANP601 3.0 0.8 1.0
O1G A:ANP601 3.0 0.2 1.0
PB A:ANP601 3.3 0.2 1.0
OD1 A:ASP494 3.4 94.0 1.0
CB A:SER373 3.5 88.1 1.0
NE2 A:GLN414 3.6 92.5 1.0
NZ A:LYS372 3.9 0.1 1.0
CG A:GLN414 3.9 98.5 1.0
N A:SER373 4.1 94.9 1.0
O1B A:ANP601 4.2 0.3 1.0
CG A:ASP494 4.2 97.1 1.0
OD2 A:ASP494 4.2 0.4 1.0
CA A:SER373 4.3 87.5 1.0
O3G A:ANP601 4.4 0.2 1.0
O3A A:ANP601 4.6 0.2 1.0
OD2 A:ASP495 4.6 0.7 1.0
O2A A:ANP601 4.6 0.7 1.0
CB A:LYS372 4.9 0.0 1.0
CG2 A:ILE524 4.9 0.7 1.0
CB A:ASP495 4.9 1.0 1.0

Reference:

M.Hohl, L.M.Hurlimann, S.Bohm, J.Schoppe, M.G.Grutter, E.Bordignon, M.A.Seeger. Structural Basis For Allosteric Cross-Talk Between the Asymmetric Nucleotide Binding Sites of A Heterodimeric Abc Exporter. Proc.Natl.Acad.Sci.Usa V. 111 11025 2014.
ISSN: ISSN 0027-8424
PubMed: 25030449
DOI: 10.1073/PNAS.1400485111
Page generated: Tue Aug 20 01:45:55 2024

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