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Magnesium in PDB 1mpo: Maltoporin Maltohexaose Complex

Protein crystallography data

The structure of Maltoporin Maltohexaose Complex, PDB code: 1mpo was solved by R.Dutzler, T.Schirmer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.80
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 129.800, 211.700, 218.200, 90.00, 90.00, 90.00
R / Rfree (%) 23 / 25.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Maltoporin Maltohexaose Complex (pdb code 1mpo). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Maltoporin Maltohexaose Complex, PDB code: 1mpo:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 1mpo

Go back to Magnesium Binding Sites List in 1mpo
Magnesium binding site 1 out of 3 in the Maltoporin Maltohexaose Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Maltoporin Maltohexaose Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg422

b:11.1
occ:0.33
MG B:MG422 0.8 11.1 0.3
MG C:MG422 0.8 11.1 0.3
OD1 C:ASP78 2.2 43.9 1.0
OD1 B:ASP78 2.5 43.9 1.0
OD2 B:ASP78 2.7 53.9 1.0
OD1 A:ASP78 2.7 43.9 1.0
OD2 C:ASP78 2.7 53.9 1.0
CG C:ASP78 2.8 40.3 1.0
CG B:ASP78 3.0 40.3 1.0
OD2 A:ASP78 3.3 53.9 1.0
CG A:ASP78 3.4 40.3 1.0
CB C:ASP78 4.3 35.0 1.0
CB B:ASP78 4.4 35.0 1.0
CB A:ASP78 4.9 35.0 1.0
CA C:ASP78 4.9 29.9 1.0

Magnesium binding site 2 out of 3 in 1mpo

Go back to Magnesium Binding Sites List in 1mpo
Magnesium binding site 2 out of 3 in the Maltoporin Maltohexaose Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Maltoporin Maltohexaose Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg422

b:11.1
occ:0.33
MG C:MG422 0.7 11.1 0.3
MG A:MG422 0.8 11.1 0.3
OD1 A:ASP78 2.2 43.9 1.0
OD1 C:ASP78 2.5 43.9 1.0
OD2 C:ASP78 2.7 53.9 1.0
OD1 B:ASP78 2.7 43.9 1.0
OD2 A:ASP78 2.7 53.9 1.0
CG A:ASP78 2.8 40.3 1.0
CG C:ASP78 3.0 40.3 1.0
OD2 B:ASP78 3.3 53.9 1.0
CG B:ASP78 3.4 40.3 1.0
CB A:ASP78 4.3 35.0 1.0
CB C:ASP78 4.4 35.0 1.0
CB B:ASP78 4.9 35.0 1.0
CA A:ASP78 4.9 29.9 1.0

Magnesium binding site 3 out of 3 in 1mpo

Go back to Magnesium Binding Sites List in 1mpo
Magnesium binding site 3 out of 3 in the Maltoporin Maltohexaose Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Maltoporin Maltohexaose Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg422

b:11.1
occ:0.33
MG B:MG422 0.7 11.1 0.3
MG A:MG422 0.8 11.1 0.3
OD1 B:ASP78 2.2 43.9 1.0
OD1 A:ASP78 2.5 43.9 1.0
OD2 A:ASP78 2.7 53.9 1.0
OD1 C:ASP78 2.7 43.9 1.0
OD2 B:ASP78 2.7 53.9 1.0
CG B:ASP78 2.8 40.3 1.0
CG A:ASP78 3.0 40.3 1.0
OD2 C:ASP78 3.3 53.9 1.0
CG C:ASP78 3.4 40.3 1.0
CB B:ASP78 4.3 35.0 1.0
CB A:ASP78 4.4 35.0 1.0
CB C:ASP78 4.9 35.0 1.0
CA B:ASP78 4.9 29.9 1.0

Reference:

R.Dutzler, Y.F.Wang, P.J.Rizkallah, J.P.Rosenbusch, T.Schirmer. Crystal Structures of Various Maltooligosaccharides Bound to Maltoporin Reveal A Specific Sugar Translocation Pathway. Structure V. 4 127 1996.
ISSN: ISSN 0969-2126
PubMed: 8805519
DOI: 10.1016/S0969-2126(96)00016-0
Page generated: Tue Aug 13 09:09:17 2024

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