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Magnesium in PDB 1ldf: Crystal Structure of the E. Coli Glycerol Facilitator (Glpf) Mutation W48F, F200T

Protein crystallography data

The structure of Crystal Structure of the E. Coli Glycerol Facilitator (Glpf) Mutation W48F, F200T, PDB code: 1ldf was solved by P.Nollert, L.J.W.Miercke, J.O'connell, R.M.Stroud, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.00 / 2.10
Space group I 4 2 2
Cell size a, b, c (Å), α, β, γ (°) 96.925, 96.925, 185.433, 90.00, 90.00, 90.00
R / Rfree (%) 23 / 24.3

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the E. Coli Glycerol Facilitator (Glpf) Mutation W48F, F200T (pdb code 1ldf). 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 the E. Coli Glycerol Facilitator (Glpf) Mutation W48F, F200T, PDB code: 1ldf:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1ldf

Go back to Magnesium Binding Sites List in 1ldf
Magnesium binding site 1 out of 2 in the Crystal Structure of the E. Coli Glycerol Facilitator (Glpf) Mutation W48F, F200T


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 the E. Coli Glycerol Facilitator (Glpf) Mutation W48F, F200T within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg301

b:21.8
occ:0.25
OE2 A:GLU43 2.4 29.0 1.0
O A:HOH522 2.5 21.6 1.0
O A:HOH531 2.5 36.2 0.2
CD A:GLU43 3.5 25.0 1.0
CG A:GLU43 4.0 24.1 1.0
O A:HOH511 4.2 44.0 1.0
OE1 A:GLU43 4.5 26.1 1.0
MG A:MG302 4.9 33.1 0.2
CD1 A:TRP42 5.0 28.3 1.0

Magnesium binding site 2 out of 2 in 1ldf

Go back to Magnesium Binding Sites List in 1ldf
Magnesium binding site 2 out of 2 in the Crystal Structure of the E. Coli Glycerol Facilitator (Glpf) Mutation W48F, F200T


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 the E. Coli Glycerol Facilitator (Glpf) Mutation W48F, F200T within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg302

b:33.1
occ:0.25
O A:HOH522 2.5 21.6 1.0
O A:HOH521 2.6 34.7 0.2
NE1 A:TRP42 3.5 30.5 1.0
CD1 A:TRP42 4.3 28.3 1.0
CE2 A:TRP42 4.6 30.0 1.0
MG A:MG301 4.9 21.8 0.2
CZ2 A:TRP42 5.0 29.0 1.0

Reference:

E.Tajkhorshid, P.Nollert, M.O.Jensen, L.J.Miercke, J.O'connell, R.M.Stroud, K.Schulten. Control of the Selectivity of the Aquaporin Water Channel Family By Global Orientational Tuning. Science V. 296 525 2002.
ISSN: ISSN 0036-8075
PubMed: 11964478
DOI: 10.1126/SCIENCE.1067778
Page generated: Tue Aug 13 08:29:31 2024

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