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Magnesium in PDB 3puy: Crystal Structure of An Outward-Facing Mbp-Maltose Transporter Complex Bound to Amp-Pnp After Crystal Soaking of the Pretranslocation State

Protein crystallography data

The structure of Crystal Structure of An Outward-Facing Mbp-Maltose Transporter Complex Bound to Amp-Pnp After Crystal Soaking of the Pretranslocation State, PDB code: 3puy was solved by M.L.Oldham, J.Chen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 3.10
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 76.550, 96.283, 112.283, 86.91, 80.87, 74.32
R / Rfree (%) 21.4 / 25.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of An Outward-Facing Mbp-Maltose Transporter Complex Bound to Amp-Pnp After Crystal Soaking of the Pretranslocation State (pdb code 3puy). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of An Outward-Facing Mbp-Maltose Transporter Complex Bound to Amp-Pnp After Crystal Soaking of the Pretranslocation State, PDB code: 3puy:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 3puy

Go back to Magnesium Binding Sites List in 3puy
Magnesium binding site 1 out of 2 in the Crystal Structure of An Outward-Facing Mbp-Maltose Transporter Complex Bound to Amp-Pnp After Crystal Soaking of the Pretranslocation State


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 An Outward-Facing Mbp-Maltose Transporter Complex Bound to Amp-Pnp After Crystal Soaking of the Pretranslocation State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1501

b:53.2
occ:1.00
O A:HOH382 1.9 33.4 1.0
O A:HOH383 1.9 77.4 1.0
OG A:SER43 2.0 41.8 1.0
O2B A:ANP2501 2.0 53.7 1.0
O1G A:ANP2501 2.1 52.1 1.0
OE1 A:GLN82 2.2 46.3 1.0
CB A:SER43 3.2 43.1 1.0
CD A:GLN82 3.2 45.6 1.0
PG A:ANP2501 3.3 52.4 1.0
PB A:ANP2501 3.4 53.2 1.0
NE2 A:GLN82 3.7 46.3 1.0
OD1 A:ASP158 3.7 46.4 1.0
N3B A:ANP2501 3.8 52.9 1.0
O3G A:ANP2501 3.9 52.6 1.0
OD2 A:ASP158 3.9 46.0 1.0
N A:SER43 3.9 44.0 1.0
O1A A:ANP2501 4.0 53.7 1.0
OE2 A:GLU159 4.0 46.8 1.0
CA A:SER43 4.1 43.7 1.0
CG A:ASP158 4.2 45.4 1.0
O3A A:ANP2501 4.3 54.1 1.0
O1B A:ANP2501 4.5 53.5 1.0
CG A:GLN82 4.5 45.2 1.0
PA A:ANP2501 4.5 54.1 1.0
N B:GLY136 4.6 46.3 1.0
O2G A:ANP2501 4.6 53.5 1.0
CB A:GLN82 4.7 45.2 1.0
O2A A:ANP2501 4.8 54.2 1.0
CE A:LYS42 4.9 41.2 1.0
CB A:LYS42 4.9 44.4 1.0
CD A:GLU159 5.0 47.0 1.0

Magnesium binding site 2 out of 2 in 3puy

Go back to Magnesium Binding Sites List in 3puy
Magnesium binding site 2 out of 2 in the Crystal Structure of An Outward-Facing Mbp-Maltose Transporter Complex Bound to Amp-Pnp After Crystal Soaking of the Pretranslocation State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of An Outward-Facing Mbp-Maltose Transporter Complex Bound to Amp-Pnp After Crystal Soaking of the Pretranslocation State within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1502

b:54.5
occ:1.00
O B:HOH383 1.9 71.0 1.0
O B:HOH382 1.9 49.8 1.0
OG B:SER43 2.0 53.3 1.0
O2B B:ANP2502 2.1 62.7 1.0
OE1 B:GLN82 2.2 47.3 1.0
O1G B:ANP2502 2.3 59.6 1.0
CB B:SER43 3.1 55.0 1.0
CD B:GLN82 3.2 47.1 1.0
PG B:ANP2502 3.4 60.1 1.0
NE2 B:GLN82 3.5 46.8 1.0
PB B:ANP2502 3.5 63.5 1.0
O3G B:ANP2502 3.7 60.1 1.0
OD1 B:ASP158 3.8 50.9 1.0
N3B B:ANP2502 3.9 62.4 1.0
OD2 B:ASP158 3.9 50.5 1.0
N B:SER43 4.0 56.3 1.0
O1A B:ANP2502 4.1 66.4 1.0
CA B:SER43 4.1 56.0 1.0
OE2 B:GLU159 4.3 51.7 1.0
CG B:ASP158 4.3 50.6 1.0
O3A B:ANP2502 4.4 65.4 1.0
CG B:GLN82 4.5 47.7 1.0
O1B B:ANP2502 4.6 64.1 1.0
PA B:ANP2502 4.6 67.0 1.0
O2A B:ANP2502 4.7 68.0 1.0
O2G B:ANP2502 4.7 60.5 1.0
N A:GLY136 4.7 54.6 1.0
CB B:GLN82 4.9 48.8 1.0
CB B:LYS42 5.0 56.0 1.0

Reference:

M.L.Oldham, J.Chen. Crystal Structure of the Maltose Transporter in A Pretranslocation Intermediate State. Science V. 332 1202 2011.
ISSN: ISSN 0036-8075
PubMed: 21566157
DOI: 10.1126/SCIENCE.1200767
Page generated: Mon Aug 11 02:12:20 2025

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