Magnesium in PDB 1wyx: The Crystal Structure of the P130CAS SH3 Domain at 1.1 A Resolution

The structure of The Crystal Structure of the P130CAS SH3 Domain at 1.1 A Resolution, PDB code: 1wyx was solved by M.Wisniewska, B.Bossenmaier, G.Georges, F.Hesse, M.Dangl, K.P.Kuenkele, I.Ioannidis, R.Huber, R.A.Engh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.10 / 1.14
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	38.071, 56.193, 37.924, 90.00, 116.22, 90.00
R / Rfree (%)	17.6 / 19.1

The binding sites of Magnesium atom in the The Crystal Structure of the P130CAS SH3 Domain at 1.1 A Resolution (pdb code 1wyx). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the The Crystal Structure of the P130CAS SH3 Domain at 1.1 A Resolution, PDB code: 1wyx:

Magnesium binding site 1 out of 1 in the The Crystal Structure of the P130CAS SH3 Domain at 1.1 A Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Crystal Structure of the P130CAS SH3 Domain at 1.1 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg181 b:13.0 occ:1.00 O A:HOH195 2.0 18.0 1.0 O B:HOH209 2.0 21.2 1.0 O B:HOH248 2.1 20.7 1.0 O B:HOH247 2.1 20.2 1.0 O B:HOH195 2.1 19.1 1.0 O A:HOH253 2.1 21.8 1.0 O A:HOH268 4.0 24.5 1.0 OD1 A:ASP11 4.0 14.9 1.0 OE1 B:GLU19 4.1 15.4 1.0 O B:HOH238 4.2 38.5 1.0 OD1 B:ASN12 4.3 18.1 1.0 OE2 B:GLU15 4.4 28.5 1.0 OD2 A:ASP11 4.5 13.8 1.0 CD A:ARG23 4.5 13.7 1.0 O B:VAL13 4.5 14.5 1.0 OE2 B:GLU19 4.6 17.8 1.0 CG A:ASP11 4.7 13.0 1.0 CD B:GLU19 4.8 15.2 1.0 CD B:GLU15 4.8 25.7 1.0 CG A:ARG23 5.0 13.6 1.0 CB A:ARG23 5.0 12.5 1.0

M.Wisniewska, B.Bossenmaier, G.Georges, F.Hesse, M.Dangl, K.P.Kunkele, I.Ioannidis, R.Huber, R.A.Engh. The 1.1 A Resolution Crystal Structure of the P130CAS SH3 Domain and Ramifications For Ligand Selectivity J.Mol.Biol. V. 347 1005 2005.
ISSN: ISSN 0022-2836
PubMed: 15784259
DOI: 10.1016/J.JMB.2005.02.017