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Magnesium in PDB 7nte: The Structure of An Open Conformation of the Sbp TARP_CSAL

Protein crystallography data

The structure of The Structure of An Open Conformation of the Sbp TARP_CSAL, PDB code: 7nte was solved by C.Bisson, R.C.Salmon, L.West, J.B.Rafferty, A.Hitchcock, G.H.Thomas, D.J.Kelly, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 53.43 / 1.60
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 63.77, 63.62, 73.7, 90, 103.39, 90
R / Rfree (%) 17.6 / 21.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the The Structure of An Open Conformation of the Sbp TARP_CSAL (pdb code 7nte). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the The Structure of An Open Conformation of the Sbp TARP_CSAL, PDB code: 7nte:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 7nte

Go back to Magnesium Binding Sites List in 7nte
Magnesium binding site 1 out of 3 in the The Structure of An Open Conformation of the Sbp TARP_CSAL


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Structure of An Open Conformation of the Sbp TARP_CSAL within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg401

b:16.1
occ:1.00
O A:HOH551 2.0 17.9 1.0
OD2 A:ASP225 2.0 21.9 1.0
O A:LYS61 2.0 16.2 1.0
OD1 A:ASP223 2.1 16.4 1.0
O A:HOH575 2.2 17.6 1.0
O A:HOH517 2.2 19.3 1.0
CG A:ASP223 3.1 16.9 1.0
CG A:ASP225 3.2 39.8 1.0
C A:LYS61 3.2 12.7 1.0
OD2 A:ASP223 3.5 14.9 1.0
CB A:ASP225 3.8 15.8 1.0
CA A:LYS61 4.0 14.8 1.0
N A:ASP225 4.2 14.9 1.0
OD1 A:ASP225 4.2 29.1 1.0
O A:HOH623 4.2 31.8 1.0
N A:ASP62 4.2 12.9 1.0
O A:GLY115 4.3 11.9 1.0
O A:HOH640 4.3 33.8 1.0
O A:ALA60 4.3 13.3 1.0
O A:HOH519 4.4 21.7 1.0
CB A:ASP223 4.5 13.7 1.0
CA A:ASP62 4.5 14.2 1.0
C A:ASP62 4.6 18.2 1.0
N A:GLY63 4.6 16.1 1.0
CA A:ASP225 4.6 18.4 1.0
N A:GLN224 4.6 11.8 1.0
CG A:LYS61 4.7 21.2 1.0
CA A:ASP223 4.8 12.7 1.0
CB A:LYS61 4.9 14.2 1.0
C A:ASP223 5.0 11.8 1.0

Magnesium binding site 2 out of 3 in 7nte

Go back to Magnesium Binding Sites List in 7nte
Magnesium binding site 2 out of 3 in the The Structure of An Open Conformation of the Sbp TARP_CSAL


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of The Structure of An Open Conformation of the Sbp TARP_CSAL within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg401

b:16.7
occ:1.00
O B:HOH523 2.0 18.9 1.0
OD2 B:ASP225 2.0 21.3 1.0
O B:HOH521 2.1 17.2 1.0
O B:LYS61 2.1 16.3 1.0
O B:HOH576 2.1 17.6 1.0
OD1 B:ASP223 2.1 12.6 1.0
CG B:ASP225 3.1 26.2 1.0
CG B:ASP223 3.1 11.7 1.0
C B:LYS61 3.2 15.4 1.0
OD2 B:ASP223 3.4 15.7 1.0
CB B:ASP225 3.7 16.3 1.0
CA B:LYS61 4.1 15.5 1.0
OD1 B:ASP225 4.1 26.4 1.0
N B:ASP225 4.1 12.3 1.0
N B:ASP62 4.2 13.8 1.0
O B:GLY115 4.3 12.1 1.0
O B:ALA60 4.4 12.6 1.0
CA B:ASP62 4.4 13.6 1.0
O B:HOH535 4.5 26.4 1.0
CB B:ASP223 4.5 12.8 1.0
N B:GLY63 4.5 18.1 1.0
C B:ASP62 4.5 19.9 1.0
CA B:ASP225 4.6 15.3 1.0
N B:GLN224 4.6 13.6 1.0
CG B:LYS61 4.7 20.7 1.0
CA B:ASP223 4.9 13.2 1.0
CB B:LYS61 5.0 18.3 1.0

Magnesium binding site 3 out of 3 in 7nte

Go back to Magnesium Binding Sites List in 7nte
Magnesium binding site 3 out of 3 in the The Structure of An Open Conformation of the Sbp TARP_CSAL


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of The Structure of An Open Conformation of the Sbp TARP_CSAL within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg402

b:37.3
occ:1.00
O B:HOH596 2.1 28.2 1.0
O B:HOH507 2.2 28.7 1.0
O B:HOH627 4.1 28.4 1.0
O B:ALA163 4.2 21.1 1.0
O B:GLY162 4.3 21.9 1.0
OE1 B:GLU164 4.5 27.8 1.0
C B:GLY162 4.6 19.9 1.0
O B:ALA159 4.6 17.7 1.0
CA B:GLY162 4.6 16.8 1.0

Reference:

C.Bisson, R.C.Salmon, L.West, J.B.Rafferty, A.Hitchcock, G.H.Thomas, D.J.Kelly. The Structural Basis For High-Affinity Uptake of Lignin-Derived Aromatic Compounds By Proteobacterial Trap Transporters. Febs J. 2021.
ISSN: ISSN 1742-464X
PubMed: 34375507
DOI: 10.1111/FEBS.16156
Page generated: Thu Oct 3 02:13:11 2024

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