Magnesium in PDB 2awo: Crystal Structure of the Adp-Mg-Bound E. Coli Malk (Crystallized with Adp-Mg)

All present enzymatic activity of Crystal Structure of the Adp-Mg-Bound E. Coli Malk (Crystallized with Adp-Mg):
3.6.3.19;

The structure of Crystal Structure of the Adp-Mg-Bound E. Coli Malk (Crystallized with Adp-Mg), PDB code: 2awo was solved by G.Lu, J.M.Westbrooks, A.L.Davidson, J.Chen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.93 / 2.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	70.213, 101.975, 131.503, 90.00, 90.73, 90.00
R / Rfree (%)	23.9 / 27.7

The binding sites of Magnesium atom in the Crystal Structure of the Adp-Mg-Bound E. Coli Malk (Crystallized with Adp-Mg) (pdb code 2awo). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Crystal Structure of the Adp-Mg-Bound E. Coli Malk (Crystallized with Adp-Mg), PDB code: 2awo:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Crystal Structure of the Adp-Mg-Bound E. Coli Malk (Crystallized with Adp-Mg)


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 Adp-Mg-Bound E. Coli Malk (Crystallized with Adp-Mg) within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg501 b:29.9 occ:1.00 OG B:SER43 2.3 31.6 1.0 O2B B:ADP402 2.5 36.5 1.0 O3B B:ADP402 3.2 33.5 1.0 CB B:SER43 3.4 29.1 1.0 PB B:ADP402 3.4 36.1 1.0 O1A B:ADP402 4.2 45.5 1.0 O3A B:ADP402 4.2 41.2 1.0 PA B:ADP402 4.4 44.9 1.0 N B:SER43 4.4 25.8 1.0 OD1 B:ASP158 4.4 37.2 1.0 CA B:SER43 4.5 28.5 1.0 O1B B:ADP402 4.7 36.5 1.0 OD2 B:ASP158 4.7 34.0 1.0 OE2 B:GLU159 4.8 39.7 1.0 CG B:ASP158 5.0 32.4 1.0

Magnesium binding site 2 out of 4 in the Crystal Structure of the Adp-Mg-Bound E. Coli Malk (Crystallized with Adp-Mg)


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 Adp-Mg-Bound E. Coli Malk (Crystallized with Adp-Mg) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg502 b:29.9 occ:1.00 OG A:SER43 2.3 41.1 1.0 O2B A:ADP401 2.8 42.2 1.0 OD1 A:ASP158 3.5 53.1 1.0 CB A:SER43 3.6 38.4 1.0 OD2 A:ASP158 3.8 45.9 1.0 O3B A:ADP401 4.0 41.0 1.0 PB A:ADP401 4.0 44.9 1.0 CG A:ASP158 4.0 48.0 1.0 OE2 A:GLU159 4.5 46.2 1.0 N A:SER43 4.6 36.7 1.0 CA A:SER43 4.6 37.5 1.0 CG A:GLU159 4.9 47.6 1.0 O3A A:ADP401 5.0 49.9 1.0

Magnesium binding site 3 out of 4 in the Crystal Structure of the Adp-Mg-Bound E. Coli Malk (Crystallized with Adp-Mg)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of the Adp-Mg-Bound E. Coli Malk (Crystallized with Adp-Mg) within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg503 b:28.8 occ:1.00 OG C:SER43 2.4 68.4 1.0 O2B C:ADP403 3.2 49.9 1.0 O3B C:ADP403 3.6 44.6 1.0 OD1 C:ASP158 3.7 72.6 1.0 CB C:SER43 3.7 68.4 1.0 PB C:ADP403 4.0 49.4 1.0 OE2 C:GLU159 4.2 87.7 1.0 OD2 C:ASP158 4.3 76.2 1.0 CG C:ASP158 4.3 72.8 1.0 N C:SER43 4.7 0.1 1.0 CA C:SER43 4.7 98.5 1.0 CG C:GLU159 4.7 86.9 1.0 O3A C:ADP403 5.0 58.1 1.0 CD C:GLU159 5.0 87.5 1.0

Magnesium binding site 4 out of 4 in the Crystal Structure of the Adp-Mg-Bound E. Coli Malk (Crystallized with Adp-Mg)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of the Adp-Mg-Bound E. Coli Malk (Crystallized with Adp-Mg) within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg504 b:33.8 occ:1.00 O2B D:ADP404 2.4 53.9 1.0 OG D:SER43 2.5 45.5 1.0 O3B D:ADP404 3.3 47.9 1.0 PB D:ADP404 3.4 51.0 1.0 CB D:SER43 3.6 48.8 1.0 O3A D:ADP404 4.3 54.0 1.0 OD2 D:ASP158 4.3 66.4 1.0 O1A D:ADP404 4.3 59.1 1.0 OD1 D:ASP158 4.3 68.2 1.0 PA D:ADP404 4.5 57.1 1.0 CG D:ASP158 4.7 68.3 1.0 O1B D:ADP404 4.7 44.9 1.0 N D:SER43 4.7 50.2 1.0 CA D:SER43 4.8 49.3 1.0

G.Lu, J.M.Westbrooks, A.L.Davidson, J.Chen. Atp Hydrolysis Is Required to Reset the Atp-Binding Cassette Dimer Into the Resting-State Conformation. Proc.Natl.Acad.Sci.Usa V. 102 17969 2005.
ISSN: ISSN 0027-8424
PubMed: 16326809
DOI: 10.1073/PNAS.0506039102