Magnesium in PDB 5yt3: Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 S218D and S222D Mutant

The structure of Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 S218D and S222D Mutant, PDB code: 5yt3 was solved by S.Nakae, K.Doko, T.Tada, T.Shirai, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	14.93 / 2.90
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	132.170, 132.550, 91.210, 90.00, 90.00, 90.00
R / Rfree (%)	20.9 / 28.9

The binding sites of Magnesium atom in the Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 S218D and S222D Mutant (pdb code 5yt3). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 S218D and S222D Mutant, PDB code: 5yt3:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 S218D and S222D Mutant


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 S218D and S222D Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg402 b:50.3 occ:1.00 O1A A:ANP401 1.9 44.8 1.0 OD1 A:ASN195 2.1 47.3 1.0 OD2 A:ASP208 2.2 80.9 1.0 O1B A:ANP401 2.3 39.7 1.0 O2G A:ANP401 2.5 44.3 1.0 PA A:ANP401 3.0 47.6 1.0 CG A:ASP208 3.2 74.5 1.0 O5' A:ANP401 3.3 45.6 1.0 CG A:ASN195 3.3 45.4 1.0 PB A:ANP401 3.4 41.0 1.0 O3A A:ANP401 3.5 47.0 1.0 O A:SER194 3.7 32.4 1.0 PG A:ANP401 3.8 52.6 1.0 CB A:ASP208 4.0 77.8 1.0 ND2 A:ASN195 4.0 47.8 1.0 OD1 A:ASP208 4.1 78.4 1.0 SG A:CYS207 4.2 60.6 1.0 N3B A:ANP401 4.2 44.1 1.0 O2A A:ANP401 4.3 47.1 1.0 C A:SER194 4.4 31.6 1.0 CB A:ASN195 4.4 38.1 1.0 CA A:ASN195 4.5 33.1 1.0 NZ A:LYS97 4.5 40.5 1.0 C5' A:ANP401 4.6 45.6 1.0 O3G A:ANP401 4.6 50.1 1.0 CE A:LYS97 4.6 37.5 1.0 O2B A:ANP401 4.7 46.2 1.0 N A:ASN195 4.7 31.6 1.0 C3' A:ANP401 4.7 48.9 1.0 C8 A:ANP401 4.7 43.8 1.0 OG A:SER194 4.8 36.9 1.0 O1G A:ANP401 4.9 43.5 1.0 CB A:SER194 4.9 31.6 1.0

Magnesium binding site 2 out of 2 in the Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 S218D and S222D Mutant


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 S218D and S222D Mutant within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg402 b:60.2 occ:1.00 OD2 C:ASP208 1.9 63.3 1.0 O1A C:ANP401 2.0 49.5 1.0 O1B C:ANP401 2.0 35.6 1.0 OD1 C:ASN195 2.1 47.5 1.0 O2G C:ANP401 2.4 41.5 1.0 PA C:ANP401 3.1 50.3 1.0 CG C:ASP208 3.1 63.5 1.0 PB C:ANP401 3.2 38.6 1.0 CG C:ASN195 3.3 48.6 1.0 O5' C:ANP401 3.4 48.0 1.0 O3A C:ANP401 3.5 45.6 1.0 O C:SER194 3.5 42.8 1.0 PG C:ANP401 3.7 51.8 1.0 CB C:ASP208 3.9 58.6 1.0 OG C:SER194 3.9 35.5 1.0 N3B C:ANP401 4.0 43.8 1.0 ND2 C:ASN195 4.0 48.9 1.0 OD1 C:ASP208 4.0 67.9 1.0 C C:SER194 4.2 36.6 1.0 SG C:CYS207 4.2 54.9 1.0 NZ C:LYS97 4.3 61.9 1.0 CB C:ASN195 4.4 40.3 1.0 O3G C:ANP401 4.5 51.9 1.0 O2B C:ANP401 4.5 51.0 1.0 CA C:ASN195 4.5 38.5 1.0 O2A C:ANP401 4.5 50.5 1.0 N C:ASN195 4.6 39.6 1.0 C5' C:ANP401 4.7 48.0 1.0 CB C:SER194 4.8 36.5 1.0 O1G C:ANP401 4.8 52.2 1.0 C3' C:ANP401 4.9 46.5 1.0

S.Nakae, K.Doko, T.Tada, T.Shirai. Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 S218D and S222D Mutant To Be Published.