Magnesium in PDB 3dgg: Crystal Structure of FABOX108

The structure of Crystal Structure of FABOX108, PDB code: 3dgg was solved by J.Ren, J.E.Nettleship, R.J.Owens, Oxford Protein Production Facility(Oppf), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.30
Space group	P 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	78.225, 52.142, 112.123, 90.00, 103.14, 90.00
R / Rfree (%)	18.7 / 24.6

The binding sites of Magnesium atom in the Crystal Structure of FABOX108 (pdb code 3dgg). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 6 binding sites of Magnesium where determined in the Crystal Structure of FABOX108, PDB code: 3dgg:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5; 6;

Magnesium binding site 1 out of 6 in the Crystal Structure of FABOX108


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 FABOX108 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg452 b:63.2 occ:1.00 NZ A:LYS43 3.5 55.2 1.0 O A:HOH543 3.7 64.1 1.0 O A:HOH504 3.9 39.0 1.0 OE1 A:GLN46 4.1 52.9 1.0 CE A:LYS43 4.2 51.9 1.0 CD A:LYS43 4.3 53.5 1.0 NZ A:LYS49 4.5 69.1 1.0 NE2 A:GLN46 4.7 56.0 1.0 NE2 A:GLN41 4.8 47.5 1.0 CD A:GLN46 4.8 58.3 1.0 CD A:LYS49 4.8 54.5 1.0

Magnesium binding site 2 out of 6 in the Crystal Structure of FABOX108


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 FABOX108 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg454 b:43.3 occ:1.00 NH1 A:ARG191 3.6 52.0 1.0 OG1 A:THR185 3.8 55.9 1.0 NH2 A:ARG191 3.8 54.1 1.0 OE1 A:GLU188 3.9 49.7 1.0 CG A:GLU188 3.9 42.3 1.0 O A:HOH560 4.0 53.0 1.0 CB A:ASP187 4.1 52.2 1.0 CZ A:ARG191 4.2 50.5 1.0 CD A:GLU188 4.3 49.5 1.0 N A:GLU188 4.6 52.5 1.0 CB A:THR185 4.8 49.2 1.0 OD2 A:ASP187 4.9 53.6 1.0 CG2 A:THR185 5.0 33.2 1.0

Magnesium binding site 3 out of 6 in the Crystal Structure of FABOX108


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 FABOX108 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg455 b:80.6 occ:1.00 NH1 A:ARG111 3.8 34.5 1.0 NH2 A:ARG111 4.2 29.6 1.0 CZ A:ARG111 4.5 29.0 1.0 O A:HOH541 4.8 73.8 1.0

Magnesium binding site 4 out of 6 in the Crystal Structure of FABOX108


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 FABOX108 within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg451 b:64.1 occ:1.00 N C:ALA9 3.7 48.9 1.0 CB C:PRO8 3.8 53.5 1.0 CA C:PRO8 4.3 50.8 1.0 CB C:ALA9 4.4 43.2 1.0 N C:SER10 4.4 48.2 1.0 C C:PRO8 4.5 49.5 1.0 CA C:ALA9 4.6 50.2 1.0 O C:SER10 4.6 44.7 1.0 O C:HOH460 4.8 56.4 1.0

Magnesium binding site 5 out of 6 in the Crystal Structure of FABOX108


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Crystal Structure of FABOX108 within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg453 b:69.7 occ:1.00 NZ C:LYS43 3.6 52.6 1.0 CE C:LYS43 3.9 49.0 1.0 CD C:LYS43 3.9 45.8 1.0 O C:HOH462 4.0 41.2 1.0 O C:HOH522 4.1 51.5 1.0 NE2 C:GLN46 4.2 50.9 1.0 OE1 C:GLN46 4.6 56.9 1.0 CD C:GLN46 4.9 51.7 1.0

Magnesium binding site 6 out of 6 in the Crystal Structure of FABOX108


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 6 of Crystal Structure of FABOX108 within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg456 b:72.8 occ:1.00 OE2 D:GLU46 3.2 55.5 1.0 N D:LYS65 3.4 54.5 1.0 OE1 D:GLU46 3.4 57.8 1.0 CB D:LYS65 3.7 57.4 1.0 CD D:GLU46 3.7 54.7 1.0 CG D:LYS65 3.7 55.9 1.0 CD2 D:PHE64 3.9 60.9 1.0 O D:HOH510 4.0 66.7 1.0 CA D:LYS65 4.1 57.8 1.0 CE2 D:PHE64 4.2 59.0 1.0 NZ D:LYS38 4.3 57.8 1.0 CA D:PHE64 4.3 55.8 1.0 C D:PHE64 4.3 54.8 1.0 N D:GLY66 4.6 57.9 1.0 CG D:PHE64 4.6 55.3 1.0 O D:HOH524 4.6 50.6 1.0 CD D:LYS38 4.7 50.2 1.0 CE D:LYS38 4.7 54.9 1.0 C D:LYS65 4.8 58.1 1.0 O D:LYS63 4.8 50.8 1.0

J.E.Nettleship, J.Ren, N.Rahman, N.S.Berrow, D.Hatherley, A.N.Barclay, R.J.Owens. A Pipeline For the Production of Antibody Fragments For Structural Studies Using Transient Expression in Hek 293T Cells. Protein Expr.Purif. V. 62 83 2008.
ISSN: ISSN 1046-5928
PubMed: 18662785
DOI: 10.1016/J.PEP.2008.06.017