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

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

The structure of Crystal Structure of the Adp-Mg-Bound E. Coli Malk (Crystallized with Atp-Mg), PDB code: 2awn 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)	37.28 / 2.30
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	70.307, 102.667, 130.776, 90.00, 90.81, 90.00
R / Rfree (%)	23 / 27.1

The binding sites of Magnesium atom in the Crystal Structure of the Adp-Mg-Bound E. Coli Malk (Crystallized with Atp-Mg) (pdb code 2awn). 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 Atp-Mg), PDB code: 2awn:
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 Atp-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 Atp-Mg) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg501 b:55.3 occ:1.00 O A:HOH607 2.0 48.9 1.0 O2B A:ADP401 2.0 50.8 1.0 O A:HOH605 2.0 49.4 1.0 O A:HOH606 2.1 58.4 1.0 OG A:SER43 2.2 57.9 1.0 O A:HOH608 2.3 67.4 1.0 CB A:SER43 3.1 56.5 1.0 PB A:ADP401 3.4 50.6 1.0 O3A A:ADP401 3.9 64.3 1.0 OE2 A:GLU159 3.9 60.5 1.0 N A:SER43 3.9 49.7 1.0 OD1 A:ASP158 4.0 61.2 1.0 O3B A:ADP401 4.0 53.7 1.0 CA A:SER43 4.1 55.4 1.0 OD2 A:ASP158 4.2 60.7 1.0 CG A:ASP158 4.5 59.8 1.0 O1B A:ADP401 4.5 38.8 1.0 CE A:LYS42 4.9 51.2 1.0 CB A:LYS42 4.9 40.2 1.0 CD A:GLU159 5.0 78.1 1.0

Magnesium binding site 2 out of 4 in the Crystal Structure of the Adp-Mg-Bound E. Coli Malk (Crystallized with Atp-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 Atp-Mg) within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg502 b:48.3 occ:1.00 O2B B:ADP402 2.0 46.1 1.0 O B:HOH603 2.2 35.9 1.0 O B:HOH602 2.2 40.1 1.0 O B:HOH604 2.2 55.4 1.0 O B:HOH601 2.2 34.4 1.0 OG B:SER43 2.3 44.8 1.0 CB B:SER43 3.4 37.8 1.0 PB B:ADP402 3.4 40.5 1.0 OE2 B:GLU159 3.8 50.0 1.0 O3A B:ADP402 3.9 48.8 1.0 O3B B:ADP402 3.9 45.1 1.0 OD1 B:ASP158 4.0 45.9 1.0 N B:SER43 4.0 33.4 1.0 OD2 B:ASP158 4.3 48.6 1.0 CA B:SER43 4.3 35.6 1.0 O1B B:ADP402 4.4 43.8 1.0 CG B:ASP158 4.5 43.8 1.0 O B:HOH732 4.8 47.6 1.0 CD B:GLU159 4.8 74.8 1.0 O B:HOH774 4.9 63.7 1.0 O B:HOH778 4.9 54.9 1.0

Magnesium binding site 3 out of 4 in the Crystal Structure of the Adp-Mg-Bound E. Coli Malk (Crystallized with Atp-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 Atp-Mg) within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg503 b:0.6 occ:1.00 OG C:SER43 2.0 0.8 1.0 O2B C:ADP403 2.3 88.0 0.5 CB C:SER43 2.9 0.1 1.0 O3B C:ADP403 3.0 85.9 0.5 PB C:ADP403 3.1 85.9 0.5 O3A C:ADP403 3.5 99.4 0.5 N C:SER43 3.7 0.2 1.0 CA C:SER43 3.9 0.8 1.0 PA C:ADP403 4.1 0.1 0.5 O1A C:ADP403 4.2 0.3 0.5 OD1 C:ASP158 4.2 96.3 1.0 O1B C:ADP403 4.5 88.7 0.5 CB C:LYS42 4.6 0.8 1.0 CE C:LYS42 4.7 99.4 1.0 C C:LYS42 4.7 0.1 1.0 OD2 C:ASP158 4.8 99.2 1.0 NZ C:LYS42 4.8 98.7 1.0 CG C:ASP158 4.9 87.9 1.0

Magnesium binding site 4 out of 4 in the Crystal Structure of the Adp-Mg-Bound E. Coli Malk (Crystallized with Atp-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 Atp-Mg) within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg504 b:76.6 occ:1.00 O D:HOH611 1.9 59.2 1.0 O D:HOH610 2.1 95.3 1.0 O2B D:ADP404 2.1 66.8 1.0 O D:HOH609 2.1 60.9 1.0 OG D:SER43 2.2 61.8 1.0 CB D:SER43 3.4 62.6 1.0 PB D:ADP404 3.4 71.4 1.0 O3B D:ADP404 3.6 71.5 1.0 OD1 D:ASP158 3.7 85.7 1.0 N D:SER43 4.1 68.1 1.0 OD2 D:ASP158 4.2 71.1 1.0 CA D:SER43 4.3 67.0 1.0 CG D:ASP158 4.4 77.6 1.0 O3A D:ADP404 4.4 55.0 1.0 OE2 D:GLU159 4.5 0.7 1.0 O1B D:ADP404 4.5 68.3 1.0 PA D:ADP404 4.7 71.4 1.0 O1A D:ADP404 4.7 67.2 1.0 CB D:LYS42 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