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Magnesium in PDB 7omt: Crystal Structure of Promacrobody 21 with Bound Maltose

Protein crystallography data

The structure of Crystal Structure of Promacrobody 21 with Bound Maltose, PDB code: 7omt was solved by M.Botte, D.Ni, S.Schenck, I.Zimmermann, M.Chami, N.Bocquet, P.Egloff, D.Bucher, M.Trabuco, R.K.Y.Cheng, J.D.Brunner, M.A.Seeger, H.Stahlberg, M.Hennig, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.45 / 2.00
Space group I 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 51.897, 87.624, 118.635, 90, 99.08, 90
R / Rfree (%) 19.3 / 23.9

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Promacrobody 21 with Bound Maltose (pdb code 7omt). 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 Promacrobody 21 with Bound Maltose, PDB code: 7omt:

Magnesium binding site 1 out of 1 in 7omt

Go back to Magnesium Binding Sites List in 7omt
Magnesium binding site 1 out of 1 in the Crystal Structure of Promacrobody 21 with Bound Maltose


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 Promacrobody 21 with Bound Maltose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg603

b:58.7
occ:1.00
O A:HOH848 2.0 56.1 0.5
O A:HOH701 2.0 49.6 1.0
OD1 A:ASP172 2.1 72.8 1.0
O A:HOH840 2.4 44.0 1.0
O A:HOH749 2.5 49.9 1.0
O A:HOH750 2.7 55.7 1.0
CG A:ASP172 2.8 67.2 1.0
OD2 A:ASP172 2.9 69.4 1.0
O A:HOH839 4.1 57.5 1.0
O A:HOH842 4.2 65.9 1.0
CB A:ASP172 4.2 61.7 1.0
N A:GLY173 4.2 41.2 1.0
O A:GLY173 4.7 42.3 1.0
CA A:ASP172 4.8 55.3 1.0
C A:ASP172 5.0 57.4 1.0

Reference:

M.Botte, D.Ni, S.Schenck, I.Zimmermann, M.Chami, N.Bocquet, P.Egloff, D.Bucher, M.Trabuco, R.K.Y.Cheng, J.D.Brunner, M.A.Seeger, H.Stahlberg, M.Hennig. Cryo-Em Structures of A Lptde Transporter in Complex with Pro-Macrobodies Offer Insight Into Lipopolysaccharide Translocation. Nat Commun V. 13 1826 2022.
ISSN: ESSN 2041-1723
PubMed: 35383177
DOI: 10.1038/S41467-022-29459-2
Page generated: Thu Oct 3 03:26:06 2024

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