Magnesium in PDB 1r3c: The Structure of P38ALPHA C162S Mutant

All present enzymatic activity of The Structure of P38ALPHA C162S Mutant:
2.7.1.37;

The structure of The Structure of P38ALPHA C162S Mutant, PDB code: 1r3c was solved by S.B.Patel, P.M.Cameron, B.Frantz-Wattley, E.O'neill, J.W.Becker, G.Scapin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	17.00 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	45.162, 84.799, 124.908, 90.00, 90.00, 90.00
R / Rfree (%)	20 / 22.4

The binding sites of Magnesium atom in the The Structure of P38ALPHA C162S Mutant (pdb code 1r3c). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the The Structure of P38ALPHA C162S Mutant, PDB code: 1r3c:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the The Structure of P38ALPHA C162S Mutant


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Structure of P38ALPHA C162S Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg2001 b:41.0 occ:1.00 O A:HOH1088 1.9 29.8 1.0 OD1 A:ASN155 2.1 25.1 1.0 OD2 A:ASP168 2.2 31.5 1.0 O A:HOH1252 2.3 37.2 1.0 O A:HOH1167 2.3 42.1 1.0 CG A:ASP168 3.2 29.7 1.0 CG A:ASN155 3.3 25.5 1.0 CB A:ASP168 3.6 28.1 1.0 ND2 A:ASN155 3.9 24.9 1.0 O A:SER154 4.0 22.8 1.0 O A:HOH1253 4.2 48.1 1.0 OG A:SER154 4.2 22.7 1.0 OD1 A:ASP168 4.3 30.2 1.0 C A:SER154 4.4 23.1 1.0 CB A:ASN155 4.5 23.8 1.0 CA A:ASN155 4.5 23.6 1.0 N A:ASN155 4.7 23.3 1.0 CB A:SER154 4.8 22.5 1.0 CE A:LYS152 4.9 24.9 1.0 CD1 A:LEU167 5.0 28.3 1.0

Magnesium binding site 2 out of 2 in the The Structure of P38ALPHA C162S Mutant


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of The Structure of P38ALPHA C162S Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg2002 b:43.3 occ:0.50 O A:HOH1097 2.1 44.2 1.0 O A:HOH1260 2.1 49.3 1.0 O A:HOH1262 2.3 54.5 1.0 OE1 A:GLU81 3.4 33.4 1.0 OE2 A:GLU81 3.8 35.6 1.0 O A:HOH1263 3.9 48.2 1.0 CD A:GLU81 3.9 32.6 1.0 OD2 A:ASP316 4.4 31.6 1.0 OD1 A:ASP316 4.8 30.4 1.0

S.B.Patel, P.M.Cameron, B.Frantz-Wattley, E.O'neill, J.W.Becker, G.Scapin. Lattice Stabilization and Enhanced Diffraction in Human P38 Alpha Crystals By Protein Engineering. Biochim.Biophys.Acta V.1696 67 2004.
ISSN: ISSN 0006-3002
PubMed: 14726206
DOI: 10.1016/J.BBAPAP.2003.09.009